1n7u

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(New page: 200px<br /><applet load="1n7u" size="450" color="white" frame="true" align="right" spinBox="true" caption="1n7u, resolution 2.40&Aring;" /> '''THE RECEPTOR-BINDING...)
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[[Image:1n7u.jpg|left|200px]]<br /><applet load="1n7u" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1n7u, resolution 2.40&Aring;" />
 
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'''THE RECEPTOR-BINDING PROTEIN P2 OF BACTERIOPHAGE PRD1: CRYSTAL FORM I'''<br />
 
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==Overview==
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==THE RECEPTOR-BINDING PROTEIN P2 OF BACTERIOPHAGE PRD1: CRYSTAL FORM I==
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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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<StructureSection load='1n7u' size='340' side='right'caption='[[1n7u]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1n7u]] 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=1N7U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1N7U FirstGlance]. <br>
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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]] 2.4&#8491;</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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1n7u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n7u OCA], [https://pdbe.org/1n7u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1n7u RCSB], [https://www.ebi.ac.uk/pdbsum/1n7u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1n7u ProSAT]</span></td></tr>
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</table>
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== Function ==
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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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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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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==About this Structure==
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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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1N7U is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_prd1 Enterobacteria phage prd1] with ACT and CA as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1N7U OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12623018 12623018]
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</div>
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[[Category: Enterobacteria phage prd1]]
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<div class="pdbe-citations 1n7u" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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== References ==
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[[Category: Bamford, D.H.]]
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<references/>
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[[Category: Benson, S.D.]]
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__TOC__
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[[Category: Burnett, R.M.]]
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</StructureSection>
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[[Category: Butcher, S.J.]]
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[[Category: Enterobacteria phage PRD1]]
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[[Category: Xu, L.]]
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[[Category: Large Structures]]
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[[Category: ACT]]
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[[Category: Bamford DH]]
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[[Category: CA]]
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[[Category: Benson SD]]
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[[Category: antibiotic-resistance]]
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[[Category: Burnett RM]]
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[[Category: bacteriophage prd1]]
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[[Category: Butcher SJ]]
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[[Category: beta-propeller]]
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[[Category: Xu L]]
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[[Category: proline-rich]]
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[[Category: viral receptor-binding]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 22:01:57 2007''
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Current revision

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

PDB ID 1n7u

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