View source for 3tbe


==The crystal structure of the complex of Streptococcus agalactiae sortase C1 and MTSET==
<StructureSection load='3tbe' size='340' side='right'caption='[[3tbe]], [[Resolution|resolution]] 2.85&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3tbe]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_agalactiae_serogroup_V Streptococcus agalactiae serogroup V]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TBE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TBE 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]] 2.85&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=ETM:2-(TRIMETHYLAMMONIUM)ETHYL+THIOL'>ETM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=3tbe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tbe OCA], [https://pdbe.org/3tbe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tbe RCSB], [https://www.ebi.ac.uk/pdbsum/3tbe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tbe ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q8E0S7_STRA5 Q8E0S7_STRA5] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
A unique feature of the class-C-type sortases, enzymes essential for Gram-positive pilus biogenesis, is the presence of a flexible "lid" anchored in the active site. However, the mechanistic details of the "lid" displacement, suggested to be a critical prelude for enzyme catalysis, are not yet known. This is partly due to the absence of enzyme-substrate and enzyme-inhibitor complex crystal structures. We have recently described the crystal structures of the Streptococcus agalactiae SAG2603 V/R sortase SrtC1 in two space groups (type II and type III) and that of its "lid" mutant and proposed a role of the "lid" as a protector of the active-site hydrophobic environment. Here, we report the crystal structures of SAG2603 V/R sortase C1 in a different space group (type I) and that of its complex with a small-molecule cysteine protease inhibitor. We observe that the catalytic Cys residue is covalently linked to the small-molecule inhibitor without lid displacement. However, the type I structure provides a view of the sortase SrtC1 lid displacement while having structural elements similar to a substrate sorting motif suitably positioned in the active site. We propose that these major conformational changes seen in the presence of a substrate mimic in the active site may represent universal features of class C sortase substrate recognition and enzyme activation.

The Crystal Structure Analysis of Group B Streptococcus Sortase C1: A Model for the "Lid" Movement upon Substrate Binding.,Khare B, Fu ZQ, Huang IH, Ton-That H, Narayana SV J Mol Biol. 2011 Oct 18. PMID:22033482<ref>PMID:22033482</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3tbe" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Streptococcus agalactiae serogroup V]]
[[Category: Khare B]]