2hlc

From Proteopedia

(Difference between revisions)

Current revision

HL COLLAGENASE STRUCTURE AT 1.7A RESOLUTION

Structural highlights

2hlc is a 2 chain structure with sequence from Hypoderma lineatum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.7Å
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/2hlc"

@@ Line 4: / Line 4: @@
 == Structural highlights ==
 <table><tr><td colspan='2'>[[2hlc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Hypoderma_lineatum Hypoderma lineatum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HLC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HLC FirstGlance]. <br>
-</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=2hlc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hlc OCA], [https://pdbe.org/2hlc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hlc RCSB], [https://www.ebi.ac.uk/pdbsum/2hlc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hlc ProSAT]</span></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</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=2hlc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hlc OCA], [https://pdbe.org/2hlc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hlc RCSB], [https://www.ebi.ac.uk/pdbsum/2hlc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hlc ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[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>
+[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]]
@@ Line 13: / Line 14: @@
   <jmolCheckbox>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hl/2hlc_consurf.spt"</scriptWhenChecked>
-    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
@@ Line 36: / Line 37: @@
 [[Category: Hypoderma lineatum]]
 [[Category: Large Structures]]
-[[Category: Arnoux, B]]
+[[Category: Arnoux B]]
-[[Category: Broutin, I]]
+[[Category: Broutin I]]
-[[Category: Ducruix, A]]
+[[Category: Ducruix A]]
-[[Category: Merigeau, K]]
+[[Category: Merigeau K]]
-[[Category: Collagen degradation]]
-[[Category: Hydrolase]]
-[[Category: Serine protease]]

2hlc

From Proteopedia

Current revision

HL COLLAGENASE STRUCTURE AT 1.7A RESOLUTION

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox