3p42

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<StructureSection load='3p42' size='340' side='right'caption='[[3p42]], [[Resolution|resolution]] 1.91&Aring;' scene=''>
<StructureSection load='3p42' size='340' side='right'caption='[[3p42]], [[Resolution|resolution]] 1.91&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3p42]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Eco27 Eco27]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3P42 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3P42 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3p42]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_O127:H6_str._E2348/69 Escherichia coli O127:H6 str. E2348/69]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3P42 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3P42 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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]] 1.91&#8491;</td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">E2348C_0970, E2348_C_0970, gfcC ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=574521 ECO27])</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=3p42 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3p42 OCA], [https://pdbe.org/3p42 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3p42 RCSB], [https://www.ebi.ac.uk/pdbsum/3p42 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3p42 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=3p42 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3p42 OCA], [https://pdbe.org/3p42 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3p42 RCSB], [https://www.ebi.ac.uk/pdbsum/3p42 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3p42 ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/B7UN63_ECO27 B7UN63_ECO27]
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We report the 1.9 A resolution crystal structure of enteropathogenic Escherichia coli GfcC, a periplasmic protein encoded by the gfc operon, which is essential for assembly of group 4 polysaccharide capsule (O-antigen capsule). Presumed gene orthologs of gfcC are present in capsule-encoding regions of at least 29 genera of Gram-negative bacteria. GfcC, a member of the DUF1017 family, is comprised of tandem beta-grasp (ubiquitin-like) domains (D2 and D3) and a carboxyl-terminal amphipathic helix, a domain arrangement reminiscent of that of Wza that forms an exit pore for group 1 capsule export. Unlike the membrane-spanning C-terminal helix from Wza, the GfcC C-terminal helix packs against D3. Previously unobserved in a beta-grasp domain structure is a 48-residue helical hairpin insert in D2 that binds to D3, constraining its position and sequestering the carboxyl-terminal amphipathic helix. A centrally located and invariant Arg115 not only is essential for proper localization but also forms one of two mostly conserved pockets. Finally, we draw analogies between a GfcC protein fused to an outer membrane beta-barrel pore in some species and fusion proteins necessary for secreting biofilm-forming exopolysaccharides.
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The Crystal Structure of Escherichia coli Group 4 Capsule Protein GfcC Reveals a Domain Organization Resembling That of Wza.,Sathiyamoorthy K, Mills E, Franzmann TM, Rosenshine I, Saper MA Biochemistry. 2011 Jun 21;50(24):5465-76. Epub 2011 May 27. PMID:21449614<ref>PMID:21449614</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>
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<div class="pdbe-citations 3p42" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Eco27]]
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[[Category: Escherichia coli O127:H6 str. E2348/69]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Saper, M A]]
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[[Category: Saper MA]]
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[[Category: Sathiyamoorthy, K]]
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[[Category: Sathiyamoorthy K]]
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[[Category: Beta-grasp]]
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[[Category: Unknown function]]
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Revision as of 11:20, 21 February 2024

Structure of GfcC (YmcB), protein encoded by the E. coli group 4 capsule operon

PDB ID 3p42

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