1n7u

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Revision as of 17:00, 7 September 2022

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

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 <StructureSection load='1n7u' size='340' side='right'caption='[[1n7u]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1n7u]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bpprd Bpprd]. 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 [http://proteopedia.org/fgij/fg.htm?mol=1N7U FirstGlance]. <br>
+<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>
 </td></tr><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>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1n7v|1n7v]]</div></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=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>
-<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 BPPRD])</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1n7u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n7u OCA], [http://pdbe.org/1n7u PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1n7u RCSB], [http://www.ebi.ac.uk/pdbsum/1n7u PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1n7u ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://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>
+[[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>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-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.
-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>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1n7u" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Bpprd]]
+[[Category: Enterobacteria phage PRD1]]
 [[Category: Large Structures]]
-[[Category: Bamford, D H]]
+[[Category: Bamford DH]]
-[[Category: Benson, S D]]
+[[Category: Benson SD]]
-[[Category: Burnett, R M]]
+[[Category: Burnett RM]]
-[[Category: Butcher, S J]]
+[[Category: Butcher SJ]]
-[[Category: Xu, L]]
+[[Category: Xu L]]
-[[Category: Antibiotic-resistance]]
-[[Category: Bacteriophage prd1]]
-[[Category: Beta-propeller]]
-[[Category: Proline-rich]]
-[[Category: Viral protein]]
-[[Category: Viral receptor-binding]]

1n7u

From Proteopedia

Revision as of 17:00, 7 September 2022

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

Structural highlights

Function

References

Contents

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