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PDBsum entry 1gen
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protein metals links
Hydrolase (metalloprotease) PDB id
1gen

 

 

 

 

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Contents
Protein chain
200 a.a. *
Metals
_NA
_ZN
_CA
_CL
Waters ×153
* Residue conservation analysis
PDB id:
1gen
Name: Hydrolase (metalloprotease)
Title: C-terminal domain of gelatinase a
Structure: Gelatinase a. Chain: a. Fragment: c-terminal domain. Synonym: mmp-2, 72kd type iv collagenase. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: human gelatinase a. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.15Å     R-factor:   0.188     R-free:   0.260
Authors: A.M.Libson,A.G.Gittis,I.E.Collier,B.L.Marmer,G.G.Goldberg,E.E.Lattman
Key ref: A.M.Libson et al. (1995). Crystal structure of the haemopexin-like C-terminal domain of gelatinase A. Nat Struct Biol, 2, 938-942. PubMed id: 7583664
Date:
19-Jul-95     Release date:   17-Aug-96    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P08253  (MMP2_HUMAN) -  72 kDa type IV collagenase from Homo sapiens
Seq:
Struc: 		 
Seq:
Struc: 		660 a.a.
200 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.3.4.24.24  - gelatinase A.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Cleavage of gelatin type I and collagen types IV, V, VII, X. Cleaves the collagen-like sequence Pro-Gln-Gly-|-Ile-Ala-Gly-Gln.
      Cofactor: Ca(2+); Zn(2+)

 

 
Nat Struct Biol 2:938-942 (1995)
PubMed id: 7583664  
 
 
Crystal structure of the haemopexin-like C-terminal domain of gelatinase A.
A.M.Libson, A.G.Gittis, I.E.Collier, B.L.Marmer, G.I.Goldberg, E.E.Lattman.
 
  ABSTRACT  
 
The crystal structure of the haemopexin-like C-terminal domain of gelatinase A reveals that it is a four-bladed beta-propeller protein. The four blades are arranged around a channel-like opening in which Ca2+ and a Na-Cl+ ion pair are bound.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
21193411 A.Tochowicz, P.Goettig, R.Evans, R.Visse, Y.Shitomi, R.Palmisano, N.Ito, K.Richter, K.Maskos, D.Franke, D.Svergun, H.Nagase, W.Bode, and Y.Itoh (2011).
The Dimer Interface of the Membrane Type 1 Matrix Metalloproteinase Hemopexin Domain: CRYSTAL STRUCTURE AND BIOLOGICAL FUNCTIONS.
  J Biol Chem, 286, 7587-7600.
PDB code: 3c7x
18619669 G.Murphy, and H.Nagase (2008).
Progress in matrix metalloproteinase research.
  Mol Aspects Med, 29, 290-308.  
  16508116 U.V.Katre, S.M.Gaikwad, S.S.Bhagyawant, U.D.Deshpande, M.I.Khan, and C.G.Suresh (2005).
Crystallization and preliminary X-ray characterization of a lectin from Cicer arietinum (chickpea).
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 61, 141-143.  
15229884 E.S.Shih, and M.J.Hwang (2004).
Alternative alignments from comparison of protein structures.
  Proteins, 56, 519-527.  
15273299 S.Y.Reddy, and T.C.Bruice (2004).
Determination of enzyme mechanisms by molecular dynamics: studies on quinoproteins, methanol dehydrogenase, and soluble glucose dehydrogenase.
  Protein Sci, 13, 1965-1978.  
12656997 V.J.Uitto, C.M.Overall, and C.McCulloch (2003).
Proteolytic host cell enzymes in gingival crevice fluid.
  Periodontol 2000, 31, 77.  
12032297 E.Morgunova, A.Tuuttila, U.Bergmann, and K.Tryggvason (2002).
Structural insight into the complex formation of latent matrix metalloproteinase 2 with tissue inhibitor of metalloproteinase 2.
  Proc Natl Acad Sci U S A, 99, 7414-7419.
PDB code: 1gxd
11937049 Z.Jawad, and M.Paoli (2002).
Novel sequences propel familiar folds.
  Structure, 10, 447-454.  
10662694 J.Ottl, D.Gabriel, G.Murphy, V.Knäuper, Y.Tominaga, H.Nagase, M.Kröger, H.Tschesche, W.Bode, and L.Moroder (2000).
Recognition and catabolism of synthetic heterotrimeric collagen peptides by matrix metalloproteinases.
  Chem Biol, 7, 119-132.  
10644727 M.W.Olson, M.M.Bernardo, M.Pietila, D.C.Gervasi, M.Toth, L.P.Kotra, I.Massova, S.Mobashery, and R.Fridman (2000).
Characterization of the monomeric and dimeric forms of latent and active matrix metalloproteinase-9. Differential rates for activation by stromelysin 1.
  J Biol Chem, 275, 2661-2668.  
9933646 C.M.Overall, A.E.King, D.K.Sam, A.D.Ong, T.T.Lau, U.M.Wallon, Y.A.DeClerck, and J.Atherstone (1999).
Identification of the tissue inhibitor of metalloproteinases-2 (TIMP-2) binding site on the hemopexin carboxyl domain of human gelatinase A by site-directed mutagenesis. The hierarchical role in binding TIMP-2 of the unique cationic clusters of hemopexin modules III and IV.
  J Biol Chem, 274, 4421-4429.  
10356396 E.Morgunova, A.Tuuttila, U.Bergmann, M.Isupov, Y.Lindqvist, G.Schneider, and K.Tryggvason (1999).
Structure of human pro-matrix metalloproteinase-2: activation mechanism revealed.
  Science, 284, 1667-1670.
PDB code: 1ck7
10196161 G.S.Butler, S.S.Apte, F.Willenbrock, and G.Murphy (1999).
Human tissue inhibitor of metalloproteinases 3 interacts with both the N- and C-terminal domains of gelatinases A and B. Regulation by polyanions.
  J Biol Chem, 274, 10846-10851.  
10545322 K.Briknarová, A.Grishaev, L.Bányai, H.Tordai, L.Patthy, and M.Llinás (1999).
The second type II module from human matrix metalloproteinase 2: structure, function and dynamics.
  Structure, 7, 1235-1245.
PDB code: 1cxw
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.  
9422744 G.S.Butler, M.J.Butler, S.J.Atkinson, H.Will, T.Tamura, S.Schade van Westrum, T.Crabbe, J.Clements, M.P.d'Ortho, and G.Murphy (1998).
The TIMP2 membrane type 1 metalloproteinase "receptor" regulates the concentration and efficient activation of progelatinase A. A kinetic study.
  J Biol Chem, 273, 871-880.  
8990162 T.A.Springer (1997).
Folding of the N-terminal, ligand-binding region of integrin alpha-subunits into a beta-propeller domain.
  Proc Natl Acad Sci U S A, 94, 65-72.  
  9164647 J.F.Woessner (1996).
Regulation of matrilysin in the rat uterus.
  Biochem Cell Biol, 74, 777-784.  
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.

 

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