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| | <StructureSection load='1qxa' size='340' side='right'caption='[[1qxa]], [[Resolution|resolution]] 2.50Å' scene=''> | | <StructureSection load='1qxa' size='340' side='right'caption='[[1qxa]], [[Resolution|resolution]] 2.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1qxa]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"micrococcus_aureus"_(rosenbach_1884)_zopf_1885 "micrococcus aureus" (rosenbach 1884) zopf 1885]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QXA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1QXA FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1qxa]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QXA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QXA FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ETM:2-(TRIMETHYLAMMONIUM)ETHYL+THIOL'>ETM</scene></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]] 2.5Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1qwz|1qwz]], [[1qx6|1qx6]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ETM:2-(TRIMETHYLAMMONIUM)ETHYL+THIOL'>ETM</scene></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=1qxa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qxa OCA], [http://pdbe.org/1qxa PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1qxa RCSB], [http://www.ebi.ac.uk/pdbsum/1qxa PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1qxa 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=1qxa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qxa OCA], [https://pdbe.org/1qxa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qxa RCSB], [https://www.ebi.ac.uk/pdbsum/1qxa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qxa ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/SRTB_STAA8 SRTB_STAA8] Transpeptidase that anchors surface proteins to the cell wall (Probable) (PubMed:11830639, PubMed:15718231, PubMed:24519933). Recognizes and modifies its substrate by proteolytic cleavage of a C-terminal sorting signal. Following cleavage, a covalent intermediate is formed via a thioester bond between the sortase and its substrate, which is then transferred and covalently attached to the cell wall (Probable) (PubMed:24519933). This sortase recognizes an Asn-Pro-Gln-Thr-Asn (NPQTN) motif in IsdC, which is cleaved by the sortase between the threonine and aspargine residues; may only have 1 substrate in this bacterium (Probable). May be dedicated to the process of iron acquisition during bacterial infection (Probable).<ref>PMID:11830639</ref> <ref>PMID:15718231</ref> <ref>PMID:24519933</ref> <ref>PMID:11830639</ref> <ref>PMID:15718231</ref> <ref>PMID:29690584</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | <jmolCheckbox> | | <jmolCheckbox> |
| | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qx/1qxa_consurf.spt"</scriptWhenChecked> | | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qx/1qxa_consurf.spt"</scriptWhenChecked> |
| - | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> | | </jmolCheckbox> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Mazmanian, S K]] | + | [[Category: Staphylococcus aureus]] |
| - | [[Category: Narayana, S V]] | + | [[Category: Mazmanian SK]] |
| - | [[Category: Schneewind, O]] | + | [[Category: Narayana SV]] |
| - | [[Category: Zong, Y]] | + | [[Category: Schneewind O]] |
| - | [[Category: Cysteine protease]] | + | [[Category: Zong Y]] |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Sortase]]
| + | |
| - | [[Category: Transpeptidase]]
| + | |
| Structural highlights
Function
SRTB_STAA8 Transpeptidase that anchors surface proteins to the cell wall (Probable) (PubMed:11830639, PubMed:15718231, PubMed:24519933). Recognizes and modifies its substrate by proteolytic cleavage of a C-terminal sorting signal. Following cleavage, a covalent intermediate is formed via a thioester bond between the sortase and its substrate, which is then transferred and covalently attached to the cell wall (Probable) (PubMed:24519933). This sortase recognizes an Asn-Pro-Gln-Thr-Asn (NPQTN) motif in IsdC, which is cleaved by the sortase between the threonine and aspargine residues; may only have 1 substrate in this bacterium (Probable). May be dedicated to the process of iron acquisition during bacterial infection (Probable).[1] [2] [3] [4] [5] [6]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Many surface proteins of Gram-positive bacteria, which play important roles during the pathogenesis of human infections, are anchored to the cell wall envelope by a mechanism requiring sortases. Sortase B, a cysteine transpeptidase from Staphylococcus aureus, cleaves the C-terminal sorting signal of IsdC at the NPQTN motif and tethers the polypeptide to the pentaglycine cell wall cross-bridge. During catalysis, the active site cysteine of sortase and the cleaved substrate form an acyl intermediate, which is then resolved by the amino group of pentaglycine cross-bridges. We report here the crystal structures of SrtBDeltaN30 in complex with two active site inhibitors, MTSET and E64, and with the cell wall substrate analog tripleglycine. These structures reveal, for the first time, the active site disposition and the unique Cys-Arg catalytic machinery of the cysteine transpeptidase, and they also provide useful information for the future design of anti-infective agents against sortases.
The structure of sortase B, a cysteine transpeptidase that tethers surface protein to the Staphylococcus aureus cell wall.,Zong Y, Mazmanian SK, Schneewind O, Narayana SV Structure. 2004 Jan;12(1):105-12. PMID:14725770[7]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Mazmanian SK, Ton-That H, Su K, Schneewind O. An iron-regulated sortase anchors a class of surface protein during Staphylococcus aureus pathogenesis. Proc Natl Acad Sci U S A. 2002 Feb 19;99(4):2293-8. PMID:11830639 doi:10.1073/pnas.032523999
- ↑ Marraffini LA, Schneewind O. Anchor structure of staphylococcal surface proteins. V. Anchor structure of the sortase B substrate IsdC. J Biol Chem. 2005 Apr 22;280(16):16263-71. PMID:15718231 doi:10.1074/jbc.M500071200
- ↑ Jacobitz AW, Wereszczynski J, Yi SW, Amer BR, Huang GL, Nguyen AV, Sawaya MR, Jung ME, McCammon JA, Clubb RT. Structural and computational studies of the Staphylococcus aureus Sortase B-substrate complex reveal a substrate-stabilized oxyanion hole. J Biol Chem. 2014 Feb 11. PMID:24519933 doi:http://dx.doi.org/10.1074/jbc.M113.509273
- ↑ Mazmanian SK, Ton-That H, Su K, Schneewind O. An iron-regulated sortase anchors a class of surface protein during Staphylococcus aureus pathogenesis. Proc Natl Acad Sci U S A. 2002 Feb 19;99(4):2293-8. PMID:11830639 doi:10.1073/pnas.032523999
- ↑ Marraffini LA, Schneewind O. Anchor structure of staphylococcal surface proteins. V. Anchor structure of the sortase B substrate IsdC. J Biol Chem. 2005 Apr 22;280(16):16263-71. PMID:15718231 doi:10.1074/jbc.M500071200
- ↑ Wang G, Wang X, Sun L, Gao Y, Niu X, Wang H. Novel Inhibitor Discovery of Staphylococcus aureus Sortase B and the Mechanism Confirmation via Molecular Modeling. Molecules. 2018 Apr 23;23(4):977. PMID:29690584 doi:10.3390/molecules23040977
- ↑ Zong Y, Mazmanian SK, Schneewind O, Narayana SV. The structure of sortase B, a cysteine transpeptidase that tethers surface protein to the Staphylococcus aureus cell wall. Structure. 2004 Jan;12(1):105-12. PMID:14725770
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