3jqw: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image: | ==Crystal structure of Clostridium histolyticum colH collagenase collagen-binding domain 3 at 2 Angstrom resolution in presence of calcium== | ||
<StructureSection load='3jqw' size='340' side='right' caption='[[3jqw]], [[Resolution|resolution]] 2.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3jqw]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Clostridium_histolyticum Clostridium histolyticum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3JQW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3JQW FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1nqj|1nqj]], [[2o8o|2o8o]], [[3jqu|3jqu]], [[3jqx|3jqx]]</td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">colH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1498 Clostridium histolyticum])</td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Microbial_collagenase Microbial collagenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.3 3.4.24.3] </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=3jqw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3jqw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3jqw RCSB], [http://www.ebi.ac.uk/pdbsum/3jqw PDBsum]</span></td></tr> | |||
</table> | |||
== 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/jq/3jqw_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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/chain_selection.php?pdb_ID=2ata ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Clostridium histolyticum secretes collagenases, ColG and ColH that cause extensive tissue destruction in myonecrosis. The C-terminal collagen-binding domain (CBD) of collagenase is required for insoluble collagen fibril binding and subsequent collagenolysis. The high resolution crystal structures of ColG-CBD (s3b) and ColH-CBD (s3) are reported in this paper. The new X-ray structure of s3 was solved at 2.0 A resolution (R=17.4%, R(free)=23.3%), while the resolution of the previously determined s3b was extended to 1.4 A (R=17.9%, R(free)=21.0%). Despite sharing only 30% sequence identity, the molecules resemble one another closely (r.m.s.d. C(alpha) = 1.5 A). All but one residue whose sidechain chelates with Ca(2+) are conserved. The dual Ca(2+) binding site in s3 is completed by an unconserved aspartate. Differential scanning calorimetric measurements showed that s3 gains thermal stability, comparable to s3b, by binding to Ca(2+) (holo T(M)=94.1 degrees C, apo T(M)=70.2 degrees C). Holo s3 is also stabilized against chemical denaturants, urea and guanidine HCl. The three most critical residues for collagen interaction in s3b are conserved in s3. The general shape of the binding pocket is retained by altered loop structures and side chain positions. Small angle X-ray scattering data revealed that s3 also binds asymmetrically to mini-collagen. Besides the calcium-binding sites and the collagen-binding pocket, architecturally important hydrophobic residues and hydrogen-bonding network around the cis-peptide bond are well-conserved within metallopeptidase subfamily M9B. CBDs were previously shown to bind to extracellular matrix of various tissues. Compactness and extreme stability in physiological Ca(2+) concentration possibly make both CBDs suitable for targeted growth factor delivery. | |||
Structural comparison of ColH and ColG collagen-binding domains from Clostridium histolyticum.,Bauer R, Wilson JJ, Philominathan ST, Davis D, Matsushita O, Sakon J J Bacteriol. 2012 Nov 9. PMID:23144249<ref>PMID:23144249</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | ==See Also== | ||
*[[Collagenase (non-MMP)|Collagenase (non-MMP)]] | *[[Collagenase (non-MMP)|Collagenase (non-MMP)]] | ||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Clostridium histolyticum]] | [[Category: Clostridium histolyticum]] | ||
[[Category: Microbial collagenase]] | [[Category: Microbial collagenase]] | ||
[[Category: Bauer, R | [[Category: Bauer, R]] | ||
[[Category: Matsushita, O | [[Category: Matsushita, O]] | ||
[[Category: Philominathan, S T.L | [[Category: Philominathan, S T.L]] | ||
[[Category: Sakon, J | [[Category: Sakon, J]] | ||
[[Category: Beta-barrel]] | [[Category: Beta-barrel]] | ||
[[Category: Cell adhesion]] | [[Category: Cell adhesion]] | ||
[[Category: Collagen]] | [[Category: Collagen]] | ||
[[Category: Dual calcium site]] | [[Category: Dual calcium site]] | ||