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| | <StructureSection load='3tb7' size='340' side='right'caption='[[3tb7]], [[Resolution|resolution]] 2.45Å' scene=''> | | <StructureSection load='3tb7' size='340' side='right'caption='[[3tb7]], [[Resolution|resolution]] 2.45Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3tb7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_agalactiae_(serotype_v) Streptococcus agalactiae (serotype v)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TB7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TB7 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3tb7]] is a 1 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=3TB7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TB7 FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3rbk|3rbk]], [[3rbi|3rbi]], [[3rbj|3rbj]], [[3tbe|3tbe]]</div></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.45Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SAG0647 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=216466 Streptococcus agalactiae (serotype V)])</td></tr>
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| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3tb7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tb7 OCA], [https://pdbe.org/3tb7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tb7 RCSB], [https://www.ebi.ac.uk/pdbsum/3tb7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tb7 ProSAT]</span></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=3tb7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tb7 OCA], [https://pdbe.org/3tb7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tb7 RCSB], [https://www.ebi.ac.uk/pdbsum/3tb7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tb7 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| - | <div style="background-color:#fffaf0;">
| + | == Function == |
| - | == Publication Abstract from PubMed == | + | [https://www.uniprot.org/uniprot/Q8E0S7_STRA5 Q8E0S7_STRA5] |
| - | 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.
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| - | | + | |
| - | 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>
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| - | | + | |
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| + | |
| - | </div>
| + | |
| - | <div class="pdbe-citations 3tb7" style="background-color:#fffaf0;"></div>
| + | |
| - | == References ==
| + | |
| - | <references/>
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Khare, B]] | + | [[Category: Streptococcus agalactiae serogroup V]] |
| - | [[Category: Beta-barrel]] | + | [[Category: Khare B]] |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Pili biogenesis]]
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