1n7v

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==THE RECEPTOR-BINDING PROTEIN P2 OF BACTERIOPHAGE PRD1: CRYSTAL FORM III==
==THE RECEPTOR-BINDING PROTEIN P2 OF BACTERIOPHAGE PRD1: CRYSTAL FORM III==
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<StructureSection load='1n7v' size='340' side='right' caption='[[1n7v]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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<StructureSection load='1n7v' size='340' side='right'caption='[[1n7v]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1n7v]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_prd1 Enterobacteria phage prd1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N7V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1N7V FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1n7v]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Enterobacteria_phage_PRD1 Enterobacteria phage PRD1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N7V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1N7V FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</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]] 2.2&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1n7u|1n7u]]</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=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">II ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10658 Enterobacteria phage PRD1])</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=1n7v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n7v OCA], [https://pdbe.org/1n7v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1n7v RCSB], [https://www.ebi.ac.uk/pdbsum/1n7v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1n7v ProSAT]</span></td></tr>
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<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=1n7v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n7v OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1n7v RCSB], [http://www.ebi.ac.uk/pdbsum/1n7v PDBsum]</span></td></tr>
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</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/P2_BPPRD P2_BPPRD] Adsorption protein. In association with P31 and trimeric P5, forms the spike complexes located at the 5-fold vertices of the capsid. Involved in recognition and attachment to the receptor on the surface of the host. Likely triggers the processes of vertex disassembly, membrane tube formation, and subsequent DNA injection. Essential for viral infectivity.<ref>PMID:11577098</ref>
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Bacteriophage PRD1 is unusual, with an internal lipid membrane, but has striking resemblances to adenovirus that include receptor binding spikes. The PRD1 vertex complex contains P2, a 590 residue monomer that binds to receptors on antibiotic-resistant strains of E. coli and so is the functional counterpart to adenovirus fiber. P2 structures from two crystal forms, at 2.2 and 2.4 A resolution, reveal an elongated club-shaped molecule with a novel beta propeller "head" showing pseudo-6-fold symmetry. An extended loop with another novel fold forms a long "tail" containing a protruding proline-rich "fin." The head and fin structures are well suited to recognition and attachment, and the tail is likely to trigger the processes of vertex disassembly, membrane tube formation, and subsequent DNA injection.
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The receptor binding protein P2 of PRD1, a virus targeting antibiotic-resistant bacteria, has a novel fold suggesting multiple functions.,Xu L, Benson SD, Butcher SJ, Bamford DH, Burnett RM Structure. 2003 Mar;11(3):309-22. PMID:12623018<ref>PMID:12623018</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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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Enterobacteria phage prd1]]
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[[Category: Enterobacteria phage PRD1]]
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[[Category: Bamford, D H]]
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[[Category: Large Structures]]
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[[Category: Benson, S D]]
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[[Category: Bamford DH]]
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[[Category: Burnett, R M]]
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[[Category: Benson SD]]
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[[Category: Butcher, S J]]
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[[Category: Burnett RM]]
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[[Category: Xu, L]]
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[[Category: Butcher SJ]]
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[[Category: Antibiotic-resistance]]
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[[Category: Xu L]]
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[[Category: Bacteriophage prd1]]
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[[Category: Beta-propeller]]
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[[Category: Proline-rich]]
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[[Category: Viral protein]]
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[[Category: Viral receptor-binding]]
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Current revision

THE RECEPTOR-BINDING PROTEIN P2 OF BACTERIOPHAGE PRD1: CRYSTAL FORM III

PDB ID 1n7v

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