1hyl

From Proteopedia

(Difference between revisions)

Revision as of 07:31, 7 April 2021

THE 1.8 A STRUCTURE OF COLLAGENASE FROM HYPODERMA LINEATUM

Structural highlights

1hyl is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[COGS_HYPLI] This enzyme is a serine protease capable of degrading the native triple helix of collagen. Also cleaves the B chain of insulin at the 15-Leu-|-Try-16 and 22-Arg-|-Gly-23 bonds. Hydrolyzes casein, but not Px-Pro-Leu-Gly-Pro-DArg, BzArgNHPh, AcTyrNHPh, 2-naphthyl phosphate, 2-naphthyl butyrate, 2-naphthyl caprylate, 2-naphthyl myristate, L-leucine 2-2-naphthylamide, L-valine 2-naphthylamide, L-cysteine 2-naphthylamide or L-glutarylphenylalanine 2-naphthylamide.^[1] ^[2]

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

Collagenase from the fly larvae Hypoderma lineatum cleaves triple-helical collagen in a single region. It was crystallized at neutral pH in the absence of inhibitor and 1.8 A data were collected using synchrotron radiation and a Mark II prototype detector. The structure was solved by combining multiple isomorphous replacement methods and rotation translation function in real space. Refinement between 7 and 1.8 A using the program X-PLOR led to a final R factor of 16.9%. The overall fold is similar to that of other trypsin-like enzymes but the structure differs mainly by the presence of a beta-sheet at position 31-44. The two embedded molecules of the asymmetric unit are related by a pseudo twofold axis. The beta-sheet 31-44 of one molecule is involved in hydrogen bonds with binding-pocket residues of the other molecule. It thus completely prevents access to the active site. The specificity of this enzyme probably results from the position of Phe192 and Tyr99 at the entrance of the active site.

1.8 A structure of Hypoderma lineatum collagenase: a member of the serine proteinase family.,Broutin I, Arnoux B, Riche C, Lecroisey A, Keil B, Pascard C, Ducruix A Acta Crystallogr D Biol Crystallogr. 1996 Mar 1;52(Pt 2):380-92. PMID:15299709^[3]

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

References

↑ Lecroisey A, Boulard C, Keil B. Chemical and enzymatic characterization of the collagenase from the insect Hypoderma lineatum. Eur J Biochem. 1979 Nov;101(2):385-93. PMID:230030
↑ Lecroisey A, Keil B. Specificity of the collagenase from the insect Hypoderma lineatum. Eur J Biochem. 1985 Oct 1;152(1):123-30. PMID:2995028
↑ Broutin I, Arnoux B, Riche C, Lecroisey A, Keil B, Pascard C, Ducruix A. 1.8 A structure of Hypoderma lineatum collagenase: a member of the serine proteinase family. Acta Crystallogr D Biol Crystallogr. 1996 Mar 1;52(Pt 2):380-92. PMID:15299709 doi:http://dx.doi.org/10.1107/S090744499501184X

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/1hyl"

@@ Line 3: / Line 3: @@
 <StructureSection load='1hyl' size='340' side='right'caption='[[1hyl]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1hyl]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HYL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1HYL FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1hyl]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HYL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HYL FirstGlance]. <br>
-</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=1hyl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hyl OCA], [http://pdbe.org/1hyl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1hyl RCSB], [http://www.ebi.ac.uk/pdbsum/1hyl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1hyl ProSAT]</span></td></tr>
+</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=1hyl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hyl OCA], [https://pdbe.org/1hyl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hyl RCSB], [https://www.ebi.ac.uk/pdbsum/1hyl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hyl ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/COGS_HYPLI COGS_HYPLI]] This enzyme is a serine protease capable of degrading the native triple helix of collagen. Also cleaves the B chain of insulin at the 15-Leu-|-Try-16 and 22-Arg-|-Gly-23 bonds. Hydrolyzes casein, but not Px-Pro-Leu-Gly-Pro-DArg, BzArgNHPh, AcTyrNHPh, 2-naphthyl phosphate, 2-naphthyl butyrate, 2-naphthyl caprylate, 2-naphthyl myristate, L-leucine 2-2-naphthylamide, L-valine 2-naphthylamide, L-cysteine 2-naphthylamide or L-glutarylphenylalanine 2-naphthylamide.<ref>PMID:230030</ref> <ref>PMID:2995028</ref>
+[[https://www.uniprot.org/uniprot/COGS_HYPLI COGS_HYPLI]] This enzyme is a serine protease capable of degrading the native triple helix of collagen. Also cleaves the B chain of insulin at the 15-Leu-|-Try-16 and 22-Arg-|-Gly-23 bonds. Hydrolyzes casein, but not Px-Pro-Leu-Gly-Pro-DArg, BzArgNHPh, AcTyrNHPh, 2-naphthyl phosphate, 2-naphthyl butyrate, 2-naphthyl caprylate, 2-naphthyl myristate, L-leucine 2-2-naphthylamide, L-valine 2-naphthylamide, L-cysteine 2-naphthylamide or L-glutarylphenylalanine 2-naphthylamide.<ref>PMID:230030</ref> <ref>PMID:2995028</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1hyl

From Proteopedia

Revision as of 07:31, 7 April 2021

THE 1.8 A STRUCTURE OF COLLAGENASE FROM HYPODERMA LINEATUM

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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