3g9k
From Proteopedia
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| - | {{Seed}}  | ||
| - | [[Image:3g9k.png|left|200px]]  | ||
| - | <  | + | ==Crystal structure of Bacillus anthracis transpeptidase enzyme CapD==  | 
| - | + | <StructureSection load='3g9k' size='340' side='right'caption='[[3g9k]], [[Resolution|resolution]] 1.79Å' scene=''>  | |
| - | + | == Structural highlights ==  | |
| - | + | <table><tr><td colspan='2'>[[3g9k]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_anthracis Bacillus anthracis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3G9K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3G9K 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]] 1.79Å</td></tr>  | |
| - | -  | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLU:GLUTAMIC+ACID'>GLU</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=3g9k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3g9k OCA], [https://pdbe.org/3g9k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3g9k RCSB], [https://www.ebi.ac.uk/pdbsum/3g9k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3g9k ProSAT]</span></td></tr>  | |
| + | </table>  | ||
| + | == Function ==  | ||
| + | [https://www.uniprot.org/uniprot/CAPD_BACAN CAPD_BACAN] Degradation of the high-molecular weight capsule (H-capsule) to the lower-molecular weight capsule (L-capsule), which is released from the bacterial cell surface. The production of L-capsule is essential to mediate escape from host defenses. Does not have gamma-glutamyltranspeptidase (GGT) activity.<ref>PMID:8105361</ref> <ref>PMID:12134259</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/g9/3g9k_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/main_output.php?pdb_ID=3g9k ConSurf].  | ||
| + | <div style="clear:both"></div>  | ||
| + | <div style="background-color:#fffaf0;">  | ||
| + | == Publication Abstract from PubMed ==  | ||
| + | Bacillus anthracis elaborates a poly-gamma-d-glutamic acid capsule that protects bacilli from phagocytic killing during infection. The enzyme CapD generates amide bonds with peptidoglycan cross-bridges to anchor capsular material within the cell wall envelope of B. anthracis. The capsular biosynthetic pathway is essential for virulence during anthrax infections and can be targeted for anti-infective inhibition with small molecules. Here, we present the crystal structures of the gamma-glutamyltranspeptidase CapD with and without alpha-l-Glu-l-Glu dipeptide, a non-hydrolyzable analog of poly-gamma-d-glutamic acid, in the active site. Purified CapD displays transpeptidation activity in vitro, and its structure reveals an active site broadly accessible for poly-gamma-glutamate binding and processing. Using structural and biochemical information, we derive a mechanistic model for CapD catalysis whereby Pro(427), Gly(428), and Gly(429) activate the catalytic residue of the enzyme, Thr(352), and stabilize an oxyanion hole via main chain amide hydrogen bonds.  | ||
| - | + | Crystal structure of Bacillus anthracis transpeptidase enzyme CapD.,Wu R, Richter S, Zhang RG, Anderson VJ, Missiakas D, Joachimiak A J Biol Chem. 2009 Sep 4;284(36):24406-14. Epub 2009 Jun 16. PMID:19535342<ref>PMID:19535342</ref>  | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>  | |
| - | + | </div>  | |
| - | + | <div class="pdbe-citations 3g9k" style="background-color:#fffaf0;"></div>  | |
| - | + | == References ==  | |
| - | + | <references/>  | |
| - | + | __TOC__  | |
| - | + | </StructureSection>  | |
| - | ==  | + | |
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| - | ==  | + | |
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[[Category: Bacillus anthracis]]  | [[Category: Bacillus anthracis]]  | ||
| - | [[Category:   | + | [[Category: Large Structures]]  | 
| - | [[Category:   | + | [[Category: Anderson VJ]]  | 
| - | + | [[Category: Joachimiak A]]  | |
| - | [[Category: Joachimiak  | + | [[Category: Missiakas D]]  | 
| - | + | [[Category: Richter S]]  | |
| - | [[Category: Missiakas  | + | [[Category: Wu R]]  | 
| - | [[Category: Richter  | + | [[Category: Zhang R]]  | 
| - | [[Category: Wu  | + | |
| - | [[Category: Zhang  | + | |
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Current revision
Crystal structure of Bacillus anthracis transpeptidase enzyme CapD
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