4e2c

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4e2c]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_Typhimurium_str._LT2 Salmonella enterica subsp. enterica serovar Typhimurium str. LT2] and [https://en.wikipedia.org/wiki/Shigella_flexneri Shigella flexneri]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4E2C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4E2C FirstGlance]. <br>
<table><tr><td colspan='2'>[[4e2c]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_Typhimurium_str._LT2 Salmonella enterica subsp. enterica serovar Typhimurium str. LT2] and [https://en.wikipedia.org/wiki/Shigella_flexneri Shigella flexneri]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4E2C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4E2C FirstGlance]. <br>
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</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=4e2c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e2c OCA], [https://pdbe.org/4e2c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4e2c RCSB], [https://www.ebi.ac.uk/pdbsum/4e2c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4e2c ProSAT]</span></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</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=4e2c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e2c OCA], [https://pdbe.org/4e2c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4e2c RCSB], [https://www.ebi.ac.uk/pdbsum/4e2c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4e2c ProSAT]</span></td></tr>
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</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/WZZB_SHIFL WZZB_SHIFL]] Confers a modal distribution of chain length on the O-antigen component of lipopolysaccharide (LPS). Gives rise to a reduced number of short chain molecules and increases in numbers of longer molecules.[[https://www.uniprot.org/uniprot/WZZB_SALTY WZZB_SALTY]] Confers a modal distribution of chain length on the O-antigen component of lipopolysaccharide (LPS). Gives rise to a reduced number of short chain molecules and increases in numbers of longer molecules, with a modal value of 20.
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[https://www.uniprot.org/uniprot/WZZB_SHIFL WZZB_SHIFL] Confers a modal distribution of chain length on the O-antigen component of lipopolysaccharide (LPS). Gives rise to a reduced number of short chain molecules and increases in numbers of longer molecules.[https://www.uniprot.org/uniprot/WZZB_SALTY WZZB_SALTY] Confers a modal distribution of chain length on the O-antigen component of lipopolysaccharide (LPS). Gives rise to a reduced number of short chain molecules and increases in numbers of longer molecules, with a modal value of 20.
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== Publication Abstract from PubMed ==
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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.
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 4e2c" 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>
</StructureSection>

Current revision

Crystal Structure of the periplasmic domain of the chimeric LPS O-antigen chain length regulator protein

PDB ID 4e2c

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