4e2h
From Proteopedia
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| - | [[ | + | ==Crystal structure of the periplasmic domain of Shigella flexneri WzzB== |
| + | <StructureSection load='4e2h' size='340' side='right' caption='[[4e2h]], [[Resolution|resolution]] 2.36Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4e2h]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Shigella_flexneri Shigella flexneri]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4E2H OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4E2H FirstGlance]. <br> | ||
| + | </td></tr><tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | ||
| + | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4e29|4e29]], [[4e2c|4e2c]], [[4e2l|4e2l]]</td></tr> | ||
| + | <tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">wzzB, cld, rol, SF2089, S2210 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=623 Shigella flexneri])</td></tr> | ||
| + | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4e2h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e2h OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4e2h RCSB], [http://www.ebi.ac.uk/pdbsum/4e2h PDBsum]</span></td></tr> | ||
| + | <table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The surface O-antigen polymers of gram-negative bacteria exhibit a modal length distribution that depends on dedicated chain-length regulator periplasmic proteins (Polysaccharide Co-Polymerases, PCPs) anchored in the inner membrane by two transmembrane helices. In an attempt to determine whether structural changes underlie the O-antigen modal length specification we have determined crystal structures of several closely related PCPs, namely two chimeric PCP-1 family members solved at 1.5A and 2.6A and a wild-type PCP-1 from Shigella flexneri solved at 2.8A. The chimeric proteins form circular octamers while the wild type WzzB from Shigella flexneri was found to be an open trimer. We also present the structure of a WzzBFepE mutant, which exhibits severe attenuation in its ability to produce very long O-antigen polymers. Our findings suggest that the differences in the modal length distribution depend primarily on the surface-exposed amino acids in specific regions rather than on the differences in the oligomeric state of the PCP protomers. | ||
| - | + | Structural characterization of closely related o-antigen LPS-chain length regulators.,Kalynych S, Yao D, Magee J, Cygler M J Biol Chem. 2012 Mar 21. PMID:22437828<ref>PMID:22437828</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | + | ||
| - | == | + | |
| - | < | + | |
[[Category: Shigella flexneri]] | [[Category: Shigella flexneri]] | ||
[[Category: Cygler, M.]] | [[Category: Cygler, M.]] | ||
Revision as of 07:18, 5 June 2014
Crystal structure of the periplasmic domain of Shigella flexneri WzzB
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