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1azz

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Revision as of 06:55, 24 February 2021

FIDDLER CRAB COLLAGENASE COMPLEXED TO ECOTIN

Structural highlights

1azz is a 4 chain structure with sequence from Celuca pugilator and Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Activity:	Brachyurin, with EC number 3.4.21.32
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[COGS_UCAPU] This enzyme is a serine protease capable of degrading the native triple helix of collagen. [ECOT_ECOLI] General inhibitor of pancreatic serine proteases: inhibits chymotrypsin, trypsin, elastases, factor X, kallikrein as well as a variety of other proteases. The strength of inhibition does not appear to be correlated with a particular protease specificity.[HAMAP-Rule:MF_00706]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The crystal structure of fiddler crab collagenase complexed with the dimeric serine protease inhibitor ecotin at 2.5 A resolution reveals an extended cleft providing binding sites for at least 11 contiguous substrate residues. Comparison of the positions of nine intermolecular main chain hydrogen bonding interactions in the cleft, with the known sequences at the cleavage site of type I collagen, suggests that the protease binding loop of ecotin adopts a conformation mimicking that of the cleaved strand of collagen. A well-defined groove extending across the binding surface of the enzyme readily accommodates the two other polypeptide chains of the triple-helical substrate. These observations permit construction of a detailed molecular model for collagen recognition and cleavage by this invertebrate serine protease. Ecotin undergoes a pronounced internal structural rearrangement which permits binding in the observed conformation. The capacity for such rearrangement appears to be a key determinant of its ability to inhibit a wide range of serine proteases.

Crystal structure of an ecotin-collagenase complex suggests a model for recognition and cleavage of the collagen triple helix.,Perona JJ, Tsu CA, Craik CS, Fletterick RJ Biochemistry. 1997 May 6;36(18):5381-92. PMID:9154920^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Perona JJ, Tsu CA, Craik CS, Fletterick RJ. Crystal structure of an ecotin-collagenase complex suggests a model for recognition and cleavage of the collagen triple helix. Biochemistry. 1997 May 6;36(18):5381-92. PMID:9154920 doi:10.1021/bi9617522

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1azz"

@@ Line 3: / Line 3: @@
 <StructureSection load='1azz' size='340' side='right'caption='[[1azz]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1azz]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Celuca_pugilator Celuca pugilator] and [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AZZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1AZZ FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1azz]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Celuca_pugilator Celuca pugilator] and [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AZZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AZZ FirstGlance]. <br>
-</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Brachyurin Brachyurin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.32 3.4.21.32] </span></td></tr>
+</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Brachyurin Brachyurin], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.32 3.4.21.32] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1azz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1azz OCA], [http://pdbe.org/1azz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1azz RCSB], [http://www.ebi.ac.uk/pdbsum/1azz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1azz ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1azz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1azz OCA], [https://pdbe.org/1azz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1azz RCSB], [https://www.ebi.ac.uk/pdbsum/1azz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1azz ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/COGS_UCAPU COGS_UCAPU]] This enzyme is a serine protease capable of degrading the native triple helix of collagen. [[http://www.uniprot.org/uniprot/ECOT_ECOLI ECOT_ECOLI]] General inhibitor of pancreatic serine proteases: inhibits chymotrypsin, trypsin, elastases, factor X, kallikrein as well as a variety of other proteases. The strength of inhibition does not appear to be correlated with a particular protease specificity.[HAMAP-Rule:MF_00706]
+[[https://www.uniprot.org/uniprot/COGS_UCAPU COGS_UCAPU]] This enzyme is a serine protease capable of degrading the native triple helix of collagen. [[https://www.uniprot.org/uniprot/ECOT_ECOLI ECOT_ECOLI]] General inhibitor of pancreatic serine proteases: inhibits chymotrypsin, trypsin, elastases, factor X, kallikrein as well as a variety of other proteases. The strength of inhibition does not appear to be correlated with a particular protease specificity.[HAMAP-Rule:MF_00706]
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1azz

From Proteopedia

Revision as of 06:55, 24 February 2021

FIDDLER CRAB COLLAGENASE COMPLEXED TO ECOTIN

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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