PDBsum entry 1qji

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Hydrolase(metalloproteinase) PDB id
Jmol PyMol
Protein chain
200 a.a. *
Waters ×495
* Residue conservation analysis
PDB id:
Name: Hydrolase(metalloproteinase)
Title: Structure of astacin with a transition-state analogue inhibitor
Structure: Astacin. Chain: a. Fragment: catalytic domain. Synonym: crayfish small molecule proteinase. Other_details: in complex with a bound transition-state analogue phosphinic pseudopeptide carbobenzoxy-pro-lys-phe-y(po2)-ala-pro-ome
Source: Astacus fluviatilis. Broad-fingered crayfish. Organism_taxid: 6715. Organ: midgut gland. Cell: f-cell. Secretion: digestive fluid. Gene: astacin
2.14Å     R-factor:   0.164    
Authors: F.Grams,W.Bode,W.Stocker
Key ref: F.Grams et al. (1996). Structure of astacin with a transition-state analogue inhibitor. Nat Struct Biol, 3, 671-675. PubMed id: 8756323
24-Jun-99     Release date:   21-Jan-00    
Go to PROCHECK summary

Protein chain
Pfam   ArchSchema ?
P07584  (ASTA_ASTFL) -  Astacin
251 a.a.
200 a.a.
Key:    PfamA domain  PfamB domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.  - Astacin.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Hydrolysis of peptide bonds in substrates containing five or more amino acids, preferentially with Ala in P1', and Pro in P2'.
      Cofactor: Zn(2+)
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     proteolysis   1 term 
  Biochemical function     metallopeptidase activity     3 terms  


Nat Struct Biol 3:671-675 (1996)
PubMed id: 8756323  
Structure of astacin with a transition-state analogue inhibitor.
F.Grams, V.Dive, A.Yiotakis, I.Yiallouros, S.Vassiliou, R.Zwilling, W.Bode, W.Stöcker.
No abstract given.


Literature references that cite this PDB file's key reference

  PubMed id Reference
21478864 T.T.Nguyen, S.C.Chang, I.Evnouchidou, I.A.York, C.Zikos, K.L.Rock, A.L.Goldberg, E.Stratikos, and L.J.Stern (2011).
Structural basis for antigenic peptide precursor processing by the endoplasmic reticulum aminopeptidase ERAP1.
  Nat Struct Mol Biol, 18, 604-613.
PDB code: 3mdj
20876133 X.Gao, J.Wang, D.Q.Yu, F.Bian, B.B.Xie, X.L.Chen, B.C.Zhou, L.H.Lai, Z.X.Wang, J.W.Wu, and Y.Z.Zhang (2010).
Structural basis for the autoprocessing of zinc metalloproteases in the thermolysin family.
  Proc Natl Acad Sci U S A, 107, 17569-17574.
PDB codes: 3nqx 3nqy 3nqz
19201757 F.X.Gomis-Rüth (2009).
Catalytic domain architecture of metzincin metalloproteases.
  J Biol Chem, 284, 15353-15357.  
19609998 I.Bertini, M.Fragai, C.Luchinat, M.Melikian, and C.Venturi (2009).
Characterisation of the MMP-12-elastin adduct.
  Chemistry, 15, 7842-7845.  
19622865 M.C.Fournié-Zaluski, H.Poras, B.P.Roques, Y.Nakajima, K.Ito, and T.Yoshimoto (2009).
Structure of aminopeptidase N from Escherichia coli complexed with the transition-state analogue aminophosphinic inhibitor PL250.
  Acta Crystallogr D Biol Crystallogr, 65, 814-822.
PDB code: 2zxg
18783725 E.E.Sterchi, W.Stöcker, and J.S.Bond (2008).
Meprins, membrane-bound and secreted astacin metalloproteinases.
  Mol Aspects Med, 29, 309-328.  
17251185 E.J.Lim, S.Sampath, J.Coll-Rodriguez, J.Schmidt, K.Ray, and D.W.Rodgers (2007).
Swapping the substrate specificities of the neuropeptidases neurolysin and thimet oligopeptidase.
  J Biol Chem, 282, 9722-9732.
PDB codes: 2o36 2o3e
17976009 J.E.Bylander, G.P.Bertenshaw, G.L.Matters, S.J.Hubbard, and J.S.Bond (2007).
Human and mouse homo-oligomeric meprin A metalloendopeptidase: substrate and inhibitor specificities.
  Biol Chem, 388, 1163-1172.  
16627477 C.Tallant, R.García-Castellanos, J.Seco, U.Baumann, and F.X.Gomis-Rüth (2006).
Molecular analysis of ulilysin, the structural prototype of a new family of metzincin metalloproteases.
  J Biol Chem, 281, 17920-17928.
PDB code: 2cki
16492671 G.F.da Silva, R.L.Reuille, L.J.Ming, and B.T.Livingston (2006).
Overexpression and mechanistic characterization of blastula protease 10, a metalloprotease involved in sea urchin embryogenesis and development.
  J Biol Chem, 281, 10737-10744.  
17096442 I.Bertini, V.Calderone, M.Fragai, C.Luchinat, M.Maletta, and K.J.Yeo (2006).
Snapshots of the reaction mechanism of matrix metalloproteinases.
  Angew Chem Int Ed Engl, 45, 7952-7955.
PDB codes: 2oxu 2oxw 2oxz 2oy2 2oy4
15883972 A.G.Tzakos, and I.P.Gerothanassis (2005).
Domain-selective ligand-binding modes and atomic level pharmacophore refinement in angiotensin I converting enzyme (ACE) inhibitors.
  Chembiochem, 6, 1089-1103.  
14998993 K.Ray, C.S.Hines, J.Coll-Rodriguez, and D.W.Rodgers (2004).
Crystal structure of human thimet oligopeptidase provides insight into substrate recognition, regulation, and localization.
  J Biol Chem, 279, 20480-20489.
PDB code: 1s4b
14754895 P.Towler, B.Staker, S.G.Prasad, S.Menon, J.Tang, T.Parsons, D.Ryan, M.Fisher, D.Williams, N.A.Dales, M.A.Patane, and M.W.Pantoliano (2004).
ACE2 X-ray structures reveal a large hinge-bending motion important for inhibitor binding and catalysis.
  J Biol Chem, 279, 17996-18007.
PDB codes: 1r42 1r4l
12618183 M.Collinsová, C.Castro, T.A.Garrow, A.Yiotakis, V.Dive, and J.Jirácek (2003).
Combining combinatorial chemistry and affinity chromatography: highly selective inhibitors of human betaine: homocysteine S-methyltransferase.
  Chem Biol, 10, 113-122.  
11840526 D.Koval, V.Kasicka, J.Jirácek, M.Collinsová, and T.A.Garrow (2002).
Analysis and characterization of phosphinic pseudopeptides by capillary zone electrophoresis.
  Electrophoresis, 23, 215-222.  
11839307 J.W.Arndt, B.Hao, V.Ramakrishnan, T.Cheng, S.I.Chan, and M.K.Chan (2002).
Crystal structure of a novel carboxypeptidase from the hyperthermophilic archaeon Pyrococcus furiosus.
  Structure, 10, 215-224.
PDB codes: 1k9x 1ka2 1ka4
12042323 R.Rozenfeld, X.Iturrioz, B.Maigret, and C.Llorens-Cortes (2002).
Contribution of molecular modeling and site-directed mutagenesis to the identification of two structural residues, Arg-220 and Asp-227, in aminopeptidase A.
  J Biol Chem, 277, 29242-29252.  
11248043 C.K.Brown, K.Madauss, W.Lian, M.R.Beck, W.D.Tolbert, and D.W.Rodgers (2001).
Structure of neurolysin reveals a deep channel that limits substrate access.
  Proc Natl Acad Sci U S A, 98, 3127-3132.
PDB code: 1i1i
11179954 F.C.Portaro, M.A.Hayashi, C.L.Silva, and Camargo (2001).
Free ATP inhibits thimet oligopeptidase (EC activity, induces autophosphorylation in vitro, and controls oligopeptide degradation in macrophage.
  Eur J Biochem, 268, 887-894.  
11478903 T.Papadopoulos, J.A.Kelly, and K.Bauer (2001).
Mutational analysis of the thyrotropin-releasing hormone-degrading ectoenzyme. similarities and differences with other members of the M1 family of aminopeptidases and thermolysin.
  Biochemistry, 40, 9347-9355.  
10194346 T.Meinnel, L.Patiny, S.Ragusa, and S.Blanquet (1999).
Design and synthesis of substrate analogue inhibitors of peptide deformylase.
  Biochemistry, 38, 4287-4295.  
10200262 V.Dive, J.Cotton, A.Yiotakis, A.Michaud, S.Vassiliou, J.Jiracek, G.Vazeux, M.T.Chauvet, P.Cuniasse, and P.Corvol (1999).
RXP 407, a phosphinic peptide, is a potent inhibitor of angiotensin I converting enzyme able to differentiate between its two active sites.
  Proc Natl Acad Sci U S A, 96, 4330-4335.  
10415721 W.Bode, C.Fernandez-Catalan, F.Grams, F.X.Gomis-Rüth, H.Nagase, H.Tschesche, and K.Maskos (1999).
Insights into MMP-TIMP interactions.
  Ann N Y Acad Sci, 878, 73-91.  
  9521103 F.X.Gomis-Rüth, E.F.Meyer, L.F.Kress, and V.Politi (1998).
Structures of adamalysin II with peptidic inhibitors. Implications for the design of tumor necrosis factor alpha convertase inhibitors.
  Protein Sci, 7, 283-292.
PDB codes: 2aig 3aig
9249047 M.Betz, P.Huxley, S.J.Davies, Y.Mushtaq, M.Pieper, H.Tschesche, W.Bode, and F.X.Gomis-Rüth (1997).
1.8-A crystal structure of the catalytic domain of human neutrophil collagenase (matrix metalloproteinase-8) complexed with a peptidomimetic hydroxamate primed-side inhibitor with a distinct selectivity profile.
  Eur J Biochem, 247, 356-363.
PDB code: 1kbc
9125517 W.L.Mock, and J.Yao (1997).
Kinetic characterization of the serralysins: a divergent catalytic mechanism pertaining to astacin-type metalloproteases.
  Biochemistry, 36, 4949-4958.  
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.