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| - | | + | #REDIRECT [[7ym7]] This PDB entry is obsolete and replaced by 7ym7 |
| - | ==SseK1 mutant - F187A==
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| - | <StructureSection load='6ixk' size='340' side='right'caption='[[6ixk]], [[Resolution|resolution]] 2.20Å' scene=''>
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| - | == Structural highlights ==
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| - | <table><tr><td colspan='2'>[[6ixk]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6IXK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6IXK FirstGlance]. <br>
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| - | </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=6ixk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ixk OCA], [http://pdbe.org/6ixk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ixk RCSB], [http://www.ebi.ac.uk/pdbsum/6ixk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ixk ProSAT]</span></td></tr>
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| - | </table>
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| - | <div style="background-color:#fffaf0;">
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| - | == Publication Abstract from PubMed ==
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| - | The bacterial effector proteins SseK and NleB glycosylate host proteins on arginine residues, leading to reduced NF-kappaB-dependent responses to infection. Salmonella SseK1 and SseK2 are E. coli NleB1 orthologs that behave as NleB1-like GTs, although they differ in protein substrate specificity. Here we report that these enzymes are retaining glycosyltransferases composed of a helix-loop-helix (HLH) domain, a lid domain, and a catalytic domain. A conserved HEN motif (His-Glu-Asn) in the active site is important for enzyme catalysis and bacterial virulence. We observe differences between SseK1 and SseK2 in interactions with substrates and identify substrate residues that are critical for enzyme recognition. Long Molecular Dynamics simulations suggest that the HLH domain determines substrate specificity and the lid-domain regulates the opening of the active site. Overall, our data suggest a front-face SNi mechanism, explain differences in activities among these effectors, and have implications for future drug development against enteric pathogens.
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| - | Structural basis for arginine glycosylation of host substrates by bacterial effector proteins.,Park JB, Kim YH, Yoo Y, Kim J, Jun SH, Cho JW, El Qaidi S, Walpole S, Monaco S, Garcia-Garcia AA, Wu M, Hays MP, Hurtado-Guerrero R, Angulo J, Hardwidge PR, Shin JS, Cho HS Nat Commun. 2018 Oct 16;9(1):4283. doi: 10.1038/s41467-018-06680-6. PMID:30327479<ref>PMID:30327479</ref>
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| - | </div>
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| - | <div class="pdbe-citations 6ixk" style="background-color:#fffaf0;"></div>
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| - | == References ==
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| - | <references/>
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| - | __TOC__
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| - | </StructureSection>
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| - | [[Category: Large Structures]]
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| - | [[Category: Park, J B]]
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| - | [[Category: Glycosyltransferase]]
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| - | [[Category: Transferase]]
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