PDBsum entry 3tln

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Hydrolase (metalloproteinase) PDB id
Protein chain
316 a.a.
_CA ×4
Waters ×173
Superseded by: 8tln
PDB id:
Name: Hydrolase (metalloproteinase)
Structure: Thermolysin
Source: (Bacillus thermoproteolyticus)
Authors: B.W.Matthews,M.A.Holmes
Key ref:
M.A.Holmes and B.W.Matthews (1982). Structure of thermolysin refined at 1.6 A resolution. J Mol Biol, 160, 623-639. PubMed id: 7175940 DOI: 10.1016/0022-2836(82)90319-9
08-Feb-82     Release date:   26-May-82    
Go to PROCHECK summary

Protein chain
No UniProt id for this chain
Struc: 316 a.a.
Key:    Secondary structure  CATH domain


DOI no: 10.1016/0022-2836(82)90319-9 J Mol Biol 160:623-639 (1982)
PubMed id: 7175940  
Structure of thermolysin refined at 1.6 A resolution.
M.A.Holmes, B.W.Matthews.
No abstract given.

  Selected figure(s)  
Figure 3.
FIG. 3. Conformational diagram for the backbone of thermolysin. Residues that are outside the ``allowed'' regions for a hard-sphere model are numbered.
Figure 4.
FIG. 4. Stereo diagram illustrating the apparent thermal motion of t,he thermolysin molecule. Larger circles correspond to residues with greater apparen motion. The radius of each c~wlr l\as obtained 1)~ taking the verage R value for all atoms in that residue, subtracting a constant value of 4.0 AZ (in order to make differences in apparent motion more obvious) and drawing the circle at t,hr SO'?; probabilit? level (Johson, 196.5).
  The above figures are reprinted by permission from Elsevier: J Mol Biol (1982, 160, 623-639) copyright 1982.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
21150094 E.Menach, K.Yasukawa, and K.Inouye (2010).
Effects of site-directed mutagenesis of the loop residue of the N-terminal domain Gly117 of thermolysin on its catalytic activity.
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19685535 L.Hocharoen, and J.A.Cowan (2009).
Metallotherapeutics: novel strategies in drug design.
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19500590 L.M.Gwyn, M.M.Peak, P.De, N.S.Rahman, and K.K.Rodgers (2009).
A zinc site in the C-terminal domain of RAG1 is essential for DNA cleavage activity.
  J Mol Biol, 390, 863-878.  
18974160 M.Kusano, K.Yasukawa, and K.Inouye (2009).
Insights into the catalytic roles of the polypeptide regions in the active site of thermolysin and generation of the thermolysin variants with high activity and stability.
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19259572 M.L.Cheng, H.X.Li, L.L.Liu, H.H.Wang, Y.Zhang, and J.P.Lang (2009).
Unique formation of mono-, tetra- and nona-nuclear zinc complexes from protonolysis reactions of [Zn(dmpzm)Et2].
  Dalton Trans, (), 2012-2019.  
19152630 O.A.Adekoya, and I.Sylte (2009).
The thermolysin family (m4) of enzymes: therapeutic and biotechnological potential.
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19218412 T.Waschkowitz, S.Rockstroh, and R.Daniel (2009).
Isolation and characterization of metalloproteases with a novel domain structure by construction and screening of metagenomic libraries.
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17965168 A.P.Bitar, M.Cao, and H.Marquis (2008).
The metalloprotease of Listeria monocytogenes is activated by intramolecular autocatalysis.
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17704566 C.Oefner, S.Pierau, H.Schulz, and G.E.Dale (2007).
Structural studies of a bifunctional inhibitor of neprilysin and DPP-IV.
  Acta Crystallogr D Biol Crystallogr, 63, 975-981.
PDB code: 2qpj
17618468 N.H.Gokhale, S.Bradford, and J.A.Cowan (2007).
Stimulation and oxidative catalytic inactivation of thermolysin by copper.Cys-Gly-His-Lys.
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16294337 O.A.Adekoya, R.Helland, N.P.Willassen, and I.Sylte (2006).
Comparative sequence and structure analysis reveal features of cold adaptation of an enzyme in the thermolysin family.
  Proteins, 62, 435-449.  
15930626 M.Kamo, K.Inouye, K.Nagata, and M.Tanokura (2005).
Preliminary X-ray crystallographic analysis of thermolysin in the presence of 4 M NaCl.
  Acta Crystallogr D Biol Crystallogr, 61, 710-712.  
15752367 P.Dürrschmidt, J.Mansfeld, and R.Ulbrich-Hofmann (2005).
An engineered disulfide bridge mimics the effect of calcium to protect neutral protease against local unfolding.
  FEBS J, 272, 1523-1534.  
15836734 Y.Matsumiya, K.Nishikawa, K.Inouye, and M.Kubo (2005).
Mutational effect for stability in a conserved region of thermolysin.
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15508121 A.S.Galanis, G.A.Spyroulias, G.Pairas, E.Manessi-Zoupa, and P.Cordopatis (2004).
Solid-phase synthesis and conformational properties of angiotensin converting enzyme catalytic-site peptides: the basis for a structural study on the enzyme-substrate interaction.
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15027050 S.Swaminathan, S.Eswaramoorthy, and D.Kumaran (2004).
Structure and enzymatic activity of botulinum neurotoxins.
  Mov Disord, 19, S17-S22.  
12767125 A.S.Galanis, G.A.Spyroulias, R.Pierattelli, A.Tzakos, A.Troganis, I.P.Gerothanassis, G.Pairas, E.Manessi-Zoupa, and P.Cordopatis (2003).
Zinc binding in peptide models of angiotensin-I converting enzyme active sites studied through 1H-NMR and chemical shift perturbation mapping.
  Biopolymers, 69, 244-252.  
12595706 S.Banumathi, M.Dauter, and Z.Dauter (2003).
Phasing at high resolution using Ta6Br12 cluster.
  Acta Crystallogr D Biol Crystallogr, 59, 492-498.  
  15455040 E.Willott, and H.Q.Tran (2002).
Zinc and Manduca sexta hemocyte functions.
  J Insect Sci, 2, 6.  
12454500 J.F.Gaucher, M.Selkti, T.Prangé, and A.Tomas (2002).
The 2.2 A resolution structure of thermolysin (TLN) crystallized in the presence of potassium thiocyanate.
  Acta Crystallogr D Biol Crystallogr, 58, 2198-2200.
PDB code: 1gxw
11148046 J.E.Jackman, C.R.Raetz, and C.A.Fierke (2001).
Site-directed mutagenesis of the bacterial metalloamidase UDP-(3-O-acyl)-N-acetylglucosamine deacetylase (LpxC). Identification of the zinc binding site.
  Biochemistry, 40, 514-523.  
11560781 N.Bonvouloir, N.Lemieux, P.Crine, G.Boileau, and L.DesGroseillers (2001).
Molecular cloning, tissue distribution, and chromosomal localization of MMEL2, a gene coding for a novel human member of the neutral endopeptidase-24.11 family.
  DNA Cell Biol, 20, 493-498.  
11427942 Y.Murakami, K.Chiba, T.Oda, and A.Hirata (2001).
Novel kinetic analysis of enzymatic dipeptide synthesis: effect of pH and substrates on thermolysin catalysis.
  Biotechnol Bioeng, 74, 406-415.  
10735252 A.Coffey, B.van den Burg, R.Veltman, and T.Abee (2000).
Characteristics of the biologically active 35-kDa metalloprotease virulence factor from Listeria monocytogenes.
  J Appl Microbiol, 88, 132-141.  
10924116 B.C.Tripp, and J.G.Ferry (2000).
A structure-function study of a proton transport pathway in the gamma-class carbonic anhydrase from Methanosarcina thermophila.
  Biochemistry, 39, 9232-9240.  
10651278 A.C.English, S.H.Done, L.S.Caves, C.R.Groom, and R.E.Hubbard (1999).
Locating interaction sites on proteins: the crystal structure of thermolysin soaked in 2% to 100% isopropanol.
  Proteins, 37, 628-640.
PDB codes: 1tli 1tlx 2tli 2tlx 3tli 4tli 5tli 6tli 7tli 8tli
10555969 E.S.Day, D.Wen, E.A.Garber, J.Hong, L.S.Avedissian, P.Rayhorn, W.Shen, C.Zeng, V.R.Bailey, J.O.Reilly, J.A.Roden, C.B.Moore, K.P.Williams, A.Galdes, A.Whitty, and D.P.Baker (1999).
Zinc-dependent structural stability of human Sonic hedgehog.
  Biochemistry, 38, 14868-14880.  
10387069 J.Mansfeld, G.Vriend, B.Van den Burg, V.G.Eijsink, and R.Ulbrich-Hofmann (1999).
Probing the unfolding region in a thermolysin-like protease by site-specific immobilization.
  Biochemistry, 38, 8240-8245.  
10500120 M.S.Brown, and J.L.Goldstein (1999).
A proteolytic pathway that controls the cholesterol content of membranes, cells, and blood.
  Proc Natl Acad Sci U S A, 96, 11041-11048.  
10419520 N.G.Zelenski, R.B.Rawson, M.S.Brown, and J.L.Goldstein (1999).
Membrane topology of S2P, a protein required for intramembranous cleavage of sterol regulatory element-binding proteins.
  J Biol Chem, 274, 21973-21980.  
10347149 P.M.Cummins, A.Pabon, E.H.Margulies, and M.J.Glucksman (1999).
Zinc coordination and substrate catalysis within the neuropeptide processing enzyme endopeptidase EC Identification of active site histidine and glutamate residues.
  J Biol Chem, 274, 16003-16009.  
10363904 P.Veprek, and J.Jezek (1999).
Peptide and glycopeptide dendrimers. Part II.
  J Pept Sci, 5, 203-220.  
9753696 A.Banbula, J.Potempa, J.Travis, C.Fernandez-Catalán, K.Mann, R.Huber, W.Bode, and F.Medrano (1998).
Amino-acid sequence and three-dimensional structure of the Staphylococcus aureus metalloproteinase at 1.72 A resolution.
  Structure, 6, 1185-1193.
PDB code: 1bqb
9846875 A.Becker, I.Schlichting, W.Kabsch, D.Groche, S.Schultz, and A.F.Wagner (1998).
Iron center, substrate recognition and mechanism of peptide deformylase.
  Nat Struct Biol, 5, 1053-1058.
PDB codes: 1bs4 1bs5 1bs6 1bs8 1bsz
9565550 A.Becker, I.Schlichting, W.Kabsch, S.Schultz, and A.F.Wagner (1998).
Structure of peptide deformylase and identification of the substrate binding site.
  J Biol Chem, 273, 11413-11416.
PDB codes: 1bs7 1icj
9482837 B.Van den Burg, G.Vriend, O.R.Veltman, G.Venema, and V.G.Eijsink (1998).
Engineering an enzyme to resist boiling.
  Proc Natl Acad Sci U S A, 95, 2056-2060.  
9614121 C.Strock, M.Cavagna, W.E.Peiffer, C.Sumbilla, D.Lewis, and G.Inesi (1998).
Direct demonstration of Ca2+ binding defects in sarco-endoplasmic reticulum Ca2+ ATPase mutants overexpressed in COS-1 cells transfected with adenovirus vectors.
  J Biol Chem, 273, 15104-15109.  
  10082367 I.L.Alberts, K.Nadassy, and S.J.Wodak (1998).
Analysis of zinc binding sites in protein crystal structures.
  Protein Sci, 7, 1700-1716.  
9614713 K.Inouye, N.Mazda, and M.Kubo (1998).
Need for aromatic residue at position 115 for proteolytic activity found by site-directed mutagenesis of tryptophan 115 in thermolysin.
  Biosci Biotechnol Biochem, 62, 798-800.  
9548763 O.R.Veltman, G.Vriend, H.J.Berendsen, B.Van den Burg, G.Venema, and V.G.Eijsink (1998).
A single calcium binding site is crucial for the calcium-dependent thermal stability of thermolysin-like proteases.
  Biochemistry, 37, 5312-5319.  
9548762 O.R.Veltman, V.G.Eijsink, G.Vriend, Kreij, G.Venema, and B.Van den Burg (1998).
Probing catalytic hinge bending motions in thermolysin-like proteases by glycine --> alanine mutations.
  Biochemistry, 37, 5305-5311.  
9720222 S.Kojima, T.Kumazaki, S.Ishii, and K.Miura (1998).
Primary structure of Streptomyces griseus metalloendopeptidase II.
  Biosci Biotechnol Biochem, 62, 1392-1398.  
9484240 V.De Filippis, F.De Antoni, M.Frigo, P.Polverino de Laureto, and A.Fontana (1998).
Enhanced protein thermostability by Ala-->Aib replacement.
  Biochemistry, 37, 1686-1696.  
9188741 A.V.Efimov (1997).
Structural trees for protein superfamilies.
  Proteins, 28, 241-260.  
9241431 C.Chothia, T.Hubbard, S.Brenner, H.Barns, and A.Murzin (1997).
Protein folds in the all-beta and all-alpha classes.
  Annu Rev Biophys Biomol Struct, 26, 597-627.  
9041139 C.M.Vidaeus, C.von Kapp-Herr, W.L.Golden, R.L.Eddy, T.B.Shows, and J.C.Herr (1997).
Human fertilin beta: identification, characterization, and chromosomal mapping of an ADAM gene family member.
  Mol Reprod Dev, 46, 363-369.  
9305992 F.Conejero-Lara, C.González, M.A.Jiménez, S.Padmanabhan, P.L.Mateo, and M.Rico (1997).
NMR solution structure of the 205-316 C-terminal fragment of thermolysin. An example of dimerization coupled to partial unfolding.
  Biochemistry, 36, 11975-11983.  
9111013 J.Mansfeld, G.Vriend, B.W.Dijkstra, O.R.Veltman, B.Van den Burg, G.Venema, R.Ulbrich-Hofmann, and V.G.Eijsink (1997).
Extreme stabilization of a thermolysin-like protease by an engineered disulfide bond.
  J Biol Chem, 272, 11152-11156.  
9346299 O.R.Veltman, G.Vriend, F.Hardy, J.Mansfeld, B.van den Burg, G.Venema, and V.G.Eijsink (1997).
Mutational analysis of a surface area that is critical for the thermal stability of thermolysin-like proteases.
  Eur J Biochem, 248, 433-440.  
  9336846 S.Kumaran, D.Datta, and R.P.Roy (1997).
Conformationally driven protease-catalyzed splicing of peptide segments: V8 protease-mediated synthesis of fragments derived from thermolysin and ribonuclease A.
  Protein Sci, 6, 2233-2241.  
9071024 T.Shirai, and M.Go (1997).
Adaptive amino acid replacements accompanied by domain fusion in reverse transcriptase.
  J Mol Evol, 44, S155-S162.  
8765753 D.J.Saul, L.C.Williams, H.S.Toogood, R.M.Daniel, and P.L.Bergquist (1996).
Sequence of the gene encoding a highly thermostable neutral proteinase from Bacillus sp. strain EA1: expression in Escherichia coli and characterisation.
  Biochim Biophys Acta, 1308, 74-80.  
8639498 F.Conejero-Lara, and P.L.Mateo (1996).
Presence of a slow dimerization equilibrium on the thermal unfolding of the 205-316 thermolysin fragment at neutral pH.
  Biochemistry, 35, 3477-3486.  
  8557345 F.Jin, O.Matsushita, S.Katayama, S.Jin, C.Matsushita, J.Minami, and A.Okabe (1996).
Purification, characterization, and primary structure of Clostridium perfringens lambda-toxin, a thermolysin-like metalloprotease.
  Infect Immun, 64, 230-237.  
8987993 O.Ogut, and J.P.Jin (1996).
Expression, zinc-affinity purification, and characterization of a novel metal-binding cluster in troponin T: metal-stabilized alpha-helical structure and effects of the NH2-terminal variable region on the conformation of intact troponin T and its association with tropomyosin.
  Biochemistry, 35, 16581-16590.  
8736557 R.N.Dutnall, D.Neuhaus, and D.Rhodes (1996).
The solution structure of the first zinc finger domain of SWI5: a novel structural extension to a common fold.
  Structure, 4, 599-611.
PDB code: 1ncs
8740360 V.Dhanaraj, Q.Z.Ye, L.L.Johnson, D.J.Hupe, D.F.Ortwine, J.B.Dunbar, J.R.Rubin, A.Pavlovsky, C.Humblet, and T.L.Blundell (1996).
X-ray structure of a hydroxamate inhibitor complex of stromelysin catalytic domain and its comparison with members of the zinc metalloproteinase superfamily.
  Structure, 4, 375-386.  
7675786 D.M.van Aalten, A.Amadei, A.B.Linssen, V.G.Eijsink, G.Vriend, and H.J.Berendsen (1995).
The essential dynamics of thermolysin: confirmation of the hinge-bending motion and comparison of simulations in vacuum and water.
  Proteins, 22, 45-54.  
  8535232 D.R.Holland, A.C.Hausrath, D.Juers, and B.W.Matthews (1995).
Structural analysis of zinc substitutions in the active site of thermolysin.
  Protein Sci, 4, 1955-1965.
PDB codes: 1lna 1lnb 1lnc 1lnd 1lne 1lnf
7737183 F.Grams, P.Reinemer, J.C.Powers, T.Kleine, M.Pieper, H.Tschesche, R.Huber, and W.Bode (1995).
X-ray structures of human neutrophil collagenase complexed with peptide hydroxamate and peptide thiol inhibitors. Implications for substrate binding and rational drug design.
  Eur J Biochem, 228, 830-841.
PDB codes: 1jao 1jaq
  7773168 M.B.Swindells (1995).
A procedure for detecting structural domains in proteins.
  Protein Sci, 4, 103-112.  
7831311 N.C.Gonnella, R.Bohacek, X.Zhang, I.Kolossváry, C.G.Paris, R.Melton, C.Winter, S.I.Hu, and V.Ganu (1995).
Bioactive conformation of stromelysin inhibitors determined by transferred nuclear Overhauser effects.
  Proc Natl Acad Sci U S A, 92, 462-466.  
8539245 R.H.Stote, and M.Karplus (1995).
Zinc binding in proteins and solution: a simple but accurate nonbonded representation.
  Proteins, 23, 12-31.  
7744050 V.De Filippis, L.Vangelista, G.Schiavo, F.Tonello, and C.Montecucco (1995).
Structural studies on the zinc-endopeptidase light chain of tetanus neurotoxin.
  Eur J Biochem, 229, 61-69.  
7615554 V.Frère, F.Sourgen, M.Monnot, F.Troalen, and S.Fermandjian (1995).
A peptide fragment of human DNA topoisomerase II alpha forms a stable coiled-coil structure in solution.
  J Biol Chem, 270, 17502-17507.  
8143751 B.Van den Burg, B.W.Dijkstra, G.Vriend, B.Van der Vinne, G.Venema, and V.G.Eijsink (1994).
Protein stabilization by hydrophobic interactions at the surface.
  Eur J Biochem, 220, 981-985.  
8052127 D.R.Wetmore, S.L.Wong, and R.S.Roche (1994).
The efficiency of processing and secretion of the thermolysin-like neutral protease from Bacillus cereus does not require the whole prosequence, but does depend on the nature of the amino acid sequence in the region of the cleavage site.
  Mol Microbiol, 12, 747-759.  
8011889 G.Inesi (1994).
Teaching active transport at the turn of the twenty-first century: recent discoveries and conceptual changes.
  Biophys J, 66, 554-560.  
  8031025 J.J.Siregar, S.A.Lerner, and S.Mobashery (1994).
Purification and characterization of aminoglycoside 3'-phosphotransferase type IIa and kinetic comparison with a new mutant enzyme.
  Antimicrob Agents Chemother, 38, 641-647.  
8170944 M.Feese, D.W.Pettigrew, N.D.Meadow, S.Roseman, and S.J.Remington (1994).
Cation-promoted association of a regulatory and target protein is controlled by protein phosphorylation.
  Proc Natl Acad Sci U S A, 91, 3544-3548.
PDB codes: 1glc 1gld 1gle
8197120 S.Yamasaki, Y.Hu, T.Binz, A.Kalkuhl, H.Kurazono, T.Tamura, R.Jahn, E.Kandel, and H.Niemann (1994).
Synaptobrevin/vesicle-associated membrane protein (VAMP) of Aplysia californica: structure and proteolysis by tetanus toxin and botulinal neurotoxins type D and F.
  Proc Natl Acad Sci U S A, 91, 4688-4692.  
  7920248 X.J.Zhang, and B.W.Matthews (1994).
Conservation of solvent-binding sites in 10 crystal forms of T4 lysozyme.
  Protein Sci, 3, 1031-1039.
PDB codes: 149l 150l 151l 152l
  8302217 C.C.Häse, and R.A.Finkelstein (1993).
Bacterial extracellular zinc-containing metalloproteases.
  Microbiol Rev, 57, 823-837.  
  8223430 F.X.Gomis-Rüth, L.F.Kress, and W.Bode (1993).
First structure of a snake venom metalloproteinase: a prototype for matrix metalloproteinases/collagenases.
  EMBO J, 12, 4151-4157.
PDB code: 1iag
8456095 G.Müller, M.Gurrath, M.Kurz, and H.Kessler (1993).
Beta VI turns in peptides and proteins: a model peptide mimicry.
  Proteins, 15, 235-251.  
8229092 G.Vriend, and V.Eijsink (1993).
Prediction and analysis of structure, stability and unfolding of thermolysin-like proteases.
  J Comput Aided Mol Des, 7, 367-396.  
8436116 M.A.Jimenez, M.Bruix, C.Gonzalez, F.J.Blanco, J.L.Nieto, J.Herranz, and M.Rico (1993).
CD and 1H-NMR studies on the conformational properties of peptide fragments from the C-terminal domain of thermolysin.
  Eur J Biochem, 211, 569-581.  
8394001 M.H.Zehfus (1993).
Improved calculations of compactness and a reevaluation of continuous compact units.
  Proteins, 16, 293-300.  
  8318900 R.C.Hoffman, S.J.Horvath, and R.E.Klevit (1993).
Structures of DNA-binding mutant zinc finger domains: implications for DNA binding.
  Protein Sci, 2, 951-965.
PDB codes: 1ard 1are 1arf
8223647 R.C.Rayne, and M.O'Shea (1993).
Structural requirements for processing of pro-adipokinetic hormone I.
  Eur J Biochem, 217, 905-911.  
8248170 T.G.Wolfsberg, J.F.Bazan, C.P.Blobel, D.G.Myles, P.Primakoff, and J.M.White (1993).
The precursor region of a protein active in sperm-egg fusion contains a metalloprotease and a disintegrin domain: structural, functional, and evolutionary implications.
  Proc Natl Acad Sci U S A, 90, 10783-10787.  
1495388 D.R.Wetmore, S.L.Wong, and R.S.Roche (1992).
The role of the pro-sequence in the processing and secretion of the thermolysin-like neutral protease from Bacillus cereus.
  Mol Microbiol, 6, 1593-1604.  
1628661 M.A.Jiménez, F.J.Blanco, M.Rico, J.Santoro, J.Herranz, and J.L.Nieto (1992).
Periodic properties of proton conformational shifts in isolated protein helices. An experimental study.
  Eur J Biochem, 207, 39-49.  
1318098 M.J.Glucksman, M.Orlowski, and J.L.Roberts (1992).
Structural and functional studies of the metalloendopeptidase (EC involved in degrading gonadotropin releasing hormone.
  Biophys J, 62, 119-122.  
1633859 R.C.Garratt, and H.Jhotí (1992).
A molecular model for the tumour-associated antigen, p97, suggests a Zn-binding function.
  FEBS Lett, 305, 55-61.  
1551587 V.A.David, A.H.Deutch, A.Sloma, D.Pawlyk, A.Ally, and D.R.Durham (1992).
Cloning, sequencing and expression of the gene encoding the extracellular neutral protease, vibriolysin, of Vibrio proteolyticus.
  Gene, 112, 107-112.  
1409570 V.G.Eijsink, G.Vriend, B.van der Vinne, B.Hazes, B.van den Burg, and G.Venema (1992).
Effects of changing the interaction between subdomains on the thermostability of Bacillus neutral proteases.
  Proteins, 14, 224-236.  
1633827 W.Stark, R.A.Pauptit, K.S.Wilson, and J.N.Jansonius (1992).
The structure of neutral protease from Bacillus cereus at 0.2-nm resolution.
  Eur J Biochem, 207, 781-791.
PDB code: 1npc
  1705239 J.Mengaud, C.Geoffroy, and P.Cossart (1991).
Identification of a new operon involved in Listeria monocytogenes virulence: its first gene encodes a protein homologous to bacterial metalloproteases.
  Infect Immun, 59, 1043-1049.  
  1989886 L.S.Beese, and T.A.Steitz (1991).
Structural basis for the 3'-5' exonuclease activity of Escherichia coli DNA polymerase I: a two metal ion mechanism.
  EMBO J, 10, 25-33.  
  1917867 L.Tran, X.C.Wu, and S.L.Wong (1991).
Cloning and expression of a novel protease gene encoding an extracellular neutral protease from Bacillus subtilis.
  J Bacteriol, 173, 6364-6372.  
1654548 R.J.Todd, M.E.Van Dam, D.Casimiro, B.L.Haymore, and F.H.Arnold (1991).
Cu(II)-binding properties of a cytochrome c with a synthetic metal-binding site: His-X3-His in an alpha-helix.
  Proteins, 10, 156-161.  
2110895 G.Signor, C.Vita, A.Fontana, F.Frigerio, M.Bolognesi, S.Toma, R.Gianna, E.De Gregoriis, and G.Grandi (1990).
Structural features of neutral protease from Bacillus subtilis deduced from model-building and limited proteolysis experiments.
  Eur J Biochem, 189, 221-227.  
2377604 M.M.Yamashita, L.Wesson, G.Eisenman, and D.Eisenberg (1990).
Where metal ions bind in proteins.
  Proc Natl Acad Sci U S A, 87, 5648-5652.  
2166604 M.Nilges, G.M.Clore, and A.M.Gronenborn (1990).
1H-NMR stereospecific assignments by conformational data-base searches.
  Biopolymers, 29, 813-822.  
2395868 V.A.Roberts, B.L.Iverson, S.A.Iverson, S.J.Benkovic, R.A.Lerner, E.D.Getzoff, and J.A.Tainer (1990).
Antibody remodeling: a general solution to the design of a metal-coordination site in an antibody binding pocket.
  Proc Natl Acad Sci U S A, 87, 6654-6658.  
2715793 C.Giessner-Prettre, and O.Jacob (1989).
A theoretical study of Zn++ interacting with models of ligands present at the thermolysin active site.
  J Comput Aided Mol Des, 3, 23-37.  
2776748 C.Vita, A.Fontana, and R.Jaenicke (1989).
Folding of thermolysin fragments. Hydrodynamic properties of isolated domains and subdomains.
  Eur J Biochem, 183, 513-518.  
  2691213 M.J.Kronman (1989).
Metal-ion binding and the molecular conformational properties of alpha lactalbumin.
  Crit Rev Biochem Mol Biol, 24, 565-667.  
2771946 S.R.Presnell, and F.E.Cohen (1989).
Topological distribution of four-alpha-helix bundles.
  Proc Natl Acad Sci U S A, 86, 6592-6596.  
2832171 A.Yiotakis, A.Hatgiyannacou, V.Dive, and F.Toma (1988).
New thiol inhibitors of Clostridium histolyticum collagenase. Importance of the P3' position.
  Eur J Biochem, 172, 761-766.  
3124104 J.M.Berg (1988).
Proposed structure for the zinc-binding domains from transcription factor IIIA and related proteins.
  Proc Natl Acad Sci U S A, 85, 99.  
  2842313 R.A.Bever, and B.H.Iglewski (1988).
Molecular characterization and nucleotide sequence of the Pseudomonas aeruginosa elastase structural gene.
  J Bacteriol, 170, 4309-4314.  
3448607 H.Iijima, J.B.Dunbar, and G.R.Marshall (1987).
Calibration of effective van der Waals atomic contact radii for proteins and peptides.
  Proteins, 2, 330-339.  
3709536 D.E.Tronrud, A.F.Monzingo, and B.W.Matthews (1986).
Crystallographic structural analysis of phosphoramidates as inhibitors and transition-state analogs of thermolysin.
  Eur J Biochem, 157, 261-268.
PDB codes: 1tlp 2tmn
2411552 C.Vita, A.Fontana, and I.M.Chaiken (1985).
Folding of thermolysin fragments. Correlation between conformational stability and antigenicity of carboxyl-terminal fragments.
  Eur J Biochem, 151, 191-196.  
2988395 D.G.Hangauer, P.Gund, J.D.Andose, B.L.Bush, E.M.Fluder, E.F.McIntyre, and G.M.Smith (1985).
Modeling the mechanism of peptide cleavage by thermolysin.
  Ann N Y Acad Sci, 439, 124-139.  
2410917 I.A.Wilson, D.H.Haft, E.D.Getzoff, J.A.Tainer, R.A.Lerner, and S.Brenner (1985).
Identical short peptide sequences in unrelated proteins can have different conformations: a testing ground for theories of immune recognition.
  Proc Natl Acad Sci U S A, 82, 5255-5259.  
4054126 P.Argos, and R.Leberman (1985).
Homologies and anomalies in primary structural patterns of nucleotide binding proteins.
  Eur J Biochem, 152, 651-656.  
6574483 S.I.Wayne, and J.S.Fruton (1983).
Thermolysin-catalyzed peptide bond synthesis.
  Proc Natl Acad Sci U S A, 80, 3241-3244.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.