2hlc: Difference between revisions
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== | ==HL COLLAGENASE STRUCTURE AT 1.7A RESOLUTION== | ||
<StructureSection load='2hlc' size='340' side='right'caption='[[2hlc]], [[Resolution|resolution]] 1.70Å' scene=''> | |||
== 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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7Å</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> | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<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/initialview03.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2hlc ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== 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. | 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<ref>PMID:15299709</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2hlc" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Collagenase 3D structures|Collagenase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Hypoderma lineatum]] | [[Category: Hypoderma lineatum]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Arnoux | [[Category: Arnoux B]] | ||
[[Category: Broutin | [[Category: Broutin I]] | ||
[[Category: Ducruix | [[Category: Ducruix A]] | ||
[[Category: Merigeau | [[Category: Merigeau K]] | ||