1ocy: Difference between revisions
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==Structure of the receptor-binding domain of the bacteriophage T4 short tail fibre== | |||
<StructureSection load='1ocy' size='340' side='right' caption='[[1ocy]], [[Resolution|resolution]] 1.50Å' scene=''> | <StructureSection load='1ocy' size='340' side='right' caption='[[1ocy]], [[Resolution|resolution]] 1.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1h6w|1h6w]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1h6w|1h6w]]</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=1ocy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ocy OCA], [http://pdbe.org/1ocy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ocy RCSB], [http://www.ebi.ac.uk/pdbsum/1ocy PDBsum]</span></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=1ocy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ocy OCA], [http://pdbe.org/1ocy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ocy RCSB], [http://www.ebi.ac.uk/pdbsum/1ocy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ocy ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/oc/1ocy_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/oc/1ocy_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
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[[Category: Gielen, G]] | [[Category: Gielen, G]] | ||
[[Category: Miller, S]] | [[Category: Miller, S]] | ||
[[Category: Raaij, M J. | [[Category: Raaij, M J.van]] | ||
[[Category: Schuetz, M]] | [[Category: Schuetz, M]] | ||
[[Category: Thomassen, E]] | [[Category: Thomassen, E]] | ||
Revision as of 09:27, 7 February 2018
Structure of the receptor-binding domain of the bacteriophage T4 short tail fibreStructure of the receptor-binding domain of the bacteriophage T4 short tail fibre
Structural highlights
Function[VG12_BPT4] Structural component of the short tail fiber. Secondary adhesin that binds irreversibly to the lipopolysaccharides component on the cell surface of Escherichia coli B strains during virus attachment. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedAdsorption of T4 bacteriophage to the Escherichia coli host cell is mediated by six long and six short tail fibres. After at least three long tail fibres have bound, short tail fibres extend and bind irreversibly to the core region of the host cell lipo-polysaccharide (LPS), serving as inextensible stays during penetration of the cell envelope by the tail tube. The short tail fibres consist of a parallel, in-register, trimer of gene product 12 (gp12).X-ray crystallography at 1.5A resolution of a protease-stable fragment of gp12 generated in the presence of zinc chloride reveals the structure of the C-terminal receptor-binding domain. It has a novel "knitted" fold, consisting of three extensively intertwined monomers. It reveals a metal-binding site, containing a zinc ion coordinated by six histidine residues in an octahedral conformation. We also suggest an LPS-binding region. The structure of the receptor-binding domain of the bacteriophage T4 short tail fibre reveals a knitted trimeric metal-binding fold.,Thomassen E, Gielen G, Schutz M, Schoehn G, Abrahams JP, Miller S, van Raaij MJ J Mol Biol. 2003 Aug 8;331(2):361-73. PMID:12888344[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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