View source for 2rui


==Solution Structure of the Bacillus anthracis Sortase A-substrate Complex==
<StructureSection load='2rui' size='340' side='right'caption='[[2rui]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2rui]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_anthracis_str._Sterne Bacillus anthracis str. Sterne] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RUI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RUI FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=B27:(2R,3S)+3-AMINO-4-MERCAPTO-2-BUTANOL'>B27</scene>, <scene name='pdbligand=BOC:TERT-BUTYL+HYDROGEN+CARBONATE'>BOC</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=2rui FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rui OCA], [https://pdbe.org/2rui PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rui RCSB], [https://www.ebi.ac.uk/pdbsum/2rui PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rui ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q81V16_BACAN Q81V16_BACAN] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The endospore forming bacterium Bacillus anthracis causes lethal anthrax disease in humans and animals. The ability of this pathogen to replicate within macrophages is dependent upon the display of bacterial surface proteins attached to the cell wall by the B. anthracis Sortase A ((Ba)SrtA) enzyme. Previously, we discovered that the class A (Ba)SrtA sortase contains a unique N-terminal appendage that wraps around the body of the protein to contact the active site of the enzyme. To gain insight into its function, we determined the NMR structure of (Ba)SrtA bound to a LPXTG sorting signal analog. The structure, combined with dynamics, kinetics, and whole cell protein display data suggest that the N terminus modulates substrate access to the enzyme. We propose that it may increase the efficiency of protein display by reducing the unproductive hydrolytic cleavage of enzyme-protein covalent intermediates that form during the cell wall anchoring reaction. Notably, a key active site loop (beta7/beta8 loop) undergoes a disordered to ordered transition upon binding the sorting signal, potentially facilitating recognition of lipid II.

Structure of the Bacillus anthracis Sortase A Enzyme Bound to Its Sorting Signal: A FLEXIBLE AMINO-TERMINAL APPENDAGE MODULATES SUBSTRATE ACCESS.,Chan AH, Yi SW, Terwilliger AL, Maresso AW, Jung ME, Clubb RT J Biol Chem. 2015 Oct 16;290(42):25461-74. doi: 10.1074/jbc.M115.670984. Epub, 2015 Aug 31. PMID:26324714<ref>PMID:26324714</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2rui" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bacillus anthracis str. Sterne]]
[[Category: Large Structures]]
[[Category: Synthetic construct]]
[[Category: Chan AH]]
[[Category: Clubb RT]]
[[Category: Jung ME]]
[[Category: Yi S]]