5cuw
From Proteopedia
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<StructureSection load='5cuw' size='340' side='right'caption='[[5cuw]], [[Resolution|resolution]] 1.89Å' scene=''> | <StructureSection load='5cuw' size='340' side='right'caption='[[5cuw]], [[Resolution|resolution]] 1.89Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5cuw]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[5cuw]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_coelicolor_A3(2) Streptomyces coelicolor A3(2)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CUW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CUW FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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=5cuw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cuw OCA], [https://pdbe.org/5cuw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5cuw RCSB], [https://www.ebi.ac.uk/pdbsum/5cuw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5cuw ProSAT]</span></td></tr> | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/SRTE1_STRCO SRTE1_STRCO] Transpeptidase that anchors surface proteins to the cell wall. Recognizes both Leu-Ala-x-Thr-Gly and Leu-Pro-x-Thr-Gly, with a preference for the former. Unlike the S.aureus sortase it cleaves not only the Thr-Gly motif but also the Ala-X bond; Ala-Glu and Ala-His bonds are better substrates than the Thr-Gly motif in vitro (PubMed:22296345, PubMed:27936128). Among its possible substrates are the chaplins ChpA, ChpB and ChpC; this enzyme is less important for ChpC attachment than is SrtE2. A double knockout mutant of srtE1 and srtE2 shows a developmental defect in aerial hyphae formation more dramatic than that due to chaplin deletion (PubMed:22296345).<ref>PMID:22296345</ref> <ref>PMID:27936128</ref> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | + | [[Category: Cascio D]] | |
| - | [[Category: Cascio | + | [[Category: Clubb RT]] |
| - | [[Category: Clubb | + | [[Category: Kattke MD]] |
| - | [[Category: Kattke | + | [[Category: Sawaya MR]] |
| - | [[Category: Sawaya | + | |
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Revision as of 12:28, 14 June 2023
Crystal structure of Sortase E1 from Streptomyces coelicolor with tripeptide in the active site
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