1iag: Difference between revisions

Revision as of 14:09, 21 February 2008

FIRST STRUCTURE OF A SNAKE VENOM METALLOPROTEINASE: A PROTOTYPE FOR MATRIX METALLOPROTEINASES(SLASH)COLLAGENASES

OverviewOverview

Adamalysin II, a 24 kDa zinc endopeptidase from the snake venom of Crotalus adamanteus, is a member of a large family of metalloproteinases isolated as small proteinases or proteolytic domains of mosaic haemorrhagic proteins from various snake venoms. Homologous domains have recently been detected in multimodular mammalian reproductive tract proteins. The 2.0 A crystal structure of adamalysin II reveals an ellipsoidal molecule with a shallow active-site cleft separating a relatively irregularly folded subdomain from the calcium-binding main molecular body composed of a five-stranded beta-sheet and four alpha-helices. The folding of the peptide fragment containing the zinc-binding motif HExxHxxGxxH bears only a distant resemblance to thermolysin, but is identical to that found in astacin, with the three histidines and a water molecule (linked to the glutamic acid) likewise constituting the zinc ligand; adamalysin II lacks a fifth (tyrosine) zinc ligand, however, leaving its zinc ion tetrahedrally co-ordinated. Furthermore, adamalysin II and astacin share an identical active-site basement formed by a common Metturn. Due to their virtually identical active-site environment and similar folding topology, the snake venom metalloproteinases (hitherto called adamalysins) and the astacins (and presumably also the matrix metalloproteinases/mammalian collagenases and the Serratia proteinase-like large bacterial proteinases) might be grouped into a common superfamily with distinct differences from the thermolysin family.

About this StructureAbout this Structure

1IAG is a Single protein structure of sequence from Crotalus adamanteus with , and as ligands. Active as Adamalysin, with EC number 3.4.24.46 Full crystallographic information is available from OCA.

ReferenceReference

First structure of a snake venom metalloproteinase: a prototype for matrix metalloproteinases/collagenases., Gomis-Ruth FX, Kress LF, Bode W, EMBO J. 1993 Nov;12(11):4151-7. PMID:8223430

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 '''FIRST STRUCTURE OF A SNAKE VENOM METALLOPROTEINASE: A PROTOTYPE FOR MATRIX METALLOPROTEINASES(SLASH)COLLAGENASES'''<br />
 ==Overview==
-Adamalysin II, a 24 kDa zinc endopeptidase from the snake venom of, Crotalus adamanteus, is a member of a large family of metalloproteinases, isolated as small proteinases or proteolytic domains of mosaic, haemorrhagic proteins from various snake venoms. Homologous domains have, recently been detected in multimodular mammalian reproductive tract, proteins. The 2.0 A crystal structure of adamalysin II reveals an, ellipsoidal molecule with a shallow active-site cleft separating a, relatively irregularly folded subdomain from the calcium-binding main, molecular body composed of a five-stranded beta-sheet and four, alpha-helices. The folding of the peptide fragment containing the, zinc-binding motif HExxHxxGxxH bears only a distant resemblance to, thermolysin, but is identical to that found in astacin, with the three, histidines and a water molecule (linked to the glutamic acid) likewise, constituting the zinc ligand; adamalysin II lacks a fifth (tyrosine) zinc, ligand, however, leaving its zinc ion tetrahedrally co-ordinated., Furthermore, adamalysin II and astacin share an identical active-site, basement formed by a common Metturn. Due to their virtually identical, active-site environment and similar folding topology, the snake venom, metalloproteinases (hitherto called adamalysins) and the astacins (and, presumably also the matrix metalloproteinases/mammalian collagenases and, the Serratia proteinase-like large bacterial proteinases) might be grouped, into a common superfamily with distinct differences from the thermolysin, family.
+Adamalysin II, a 24 kDa zinc endopeptidase from the snake venom of Crotalus adamanteus, is a member of a large family of metalloproteinases isolated as small proteinases or proteolytic domains of mosaic haemorrhagic proteins from various snake venoms. Homologous domains have recently been detected in multimodular mammalian reproductive tract proteins. The 2.0 A crystal structure of adamalysin II reveals an ellipsoidal molecule with a shallow active-site cleft separating a relatively irregularly folded subdomain from the calcium-binding main molecular body composed of a five-stranded beta-sheet and four alpha-helices. The folding of the peptide fragment containing the zinc-binding motif HExxHxxGxxH bears only a distant resemblance to thermolysin, but is identical to that found in astacin, with the three histidines and a water molecule (linked to the glutamic acid) likewise constituting the zinc ligand; adamalysin II lacks a fifth (tyrosine) zinc ligand, however, leaving its zinc ion tetrahedrally co-ordinated. Furthermore, adamalysin II and astacin share an identical active-site basement formed by a common Metturn. Due to their virtually identical active-site environment and similar folding topology, the snake venom metalloproteinases (hitherto called adamalysins) and the astacins (and presumably also the matrix metalloproteinases/mammalian collagenases and the Serratia proteinase-like large bacterial proteinases) might be grouped into a common superfamily with distinct differences from the thermolysin family.
 ==About this Structure==
-IAG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Crotalus_adamanteus Crotalus adamanteus] with ZN, CA and SO4 as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Adamalysin Adamalysin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.46 3.4.24.46] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1IAG OCA].
+IAG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Crotalus_adamanteus Crotalus adamanteus] with <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Adamalysin Adamalysin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.46 3.4.24.46] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IAG OCA].
 ==Reference==
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 [[Category: Single protein]]
 [[Category: Bode, W.]]
-[[Category: Gomis-Rueth, F.X.]]
+[[Category: Gomis-Rueth, F X.]]
 [[Category: CA]]
 [[Category: SO4]]
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 [[Category: metalloprotease]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 17:13:05 2007''
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