<?xml version="1.0" encoding="UTF-8"?><?xml-stylesheet type="text/xsl" href="static/style.xsl"?><OAI-PMH xmlns="http://www.openarchives.org/OAI/2.0/" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xsi:schemaLocation="http://www.openarchives.org/OAI/2.0/ http://www.openarchives.org/OAI/2.0/OAI-PMH.xsd"><responseDate>2026-05-17T00:15:30Z</responseDate><request verb="GetRecord" identifier="oai:repisalud.isciii.es:20.500.12105/8974" metadataPrefix="marc">https://repisalud.isciii.es/rest/oai/request</request><GetRecord><record><header><identifier>oai:repisalud.isciii.es:20.500.12105/8974</identifier><datestamp>2024-09-27T22:19:28Z</datestamp><setSpec>com_20.500.12105_2052</setSpec><setSpec>com_20.500.12105_2051</setSpec><setSpec>col_20.500.12105_19609</setSpec></header><metadata><record xmlns="http://www.loc.gov/MARC21/slim" xmlns:dcterms="http://purl.org/dc/terms/" xmlns:doc="http://www.lyncode.com/xoai" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xsi:schemaLocation="http://www.loc.gov/MARC21/slim http://www.loc.gov/standards/marcxml/schema/MARC21slim.xsd">
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      <subfield code="a">Garcia-Doval, Carmela</subfield>
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      <subfield code="a">Castón, José R</subfield>
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      <subfield code="a">Luque, Daniel</subfield>
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      <subfield code="a">Granell, Meritxell</subfield>
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      <subfield code="a">Otero, José M</subfield>
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      <subfield code="a">Llamas-Saiz, Antonio L</subfield>
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      <subfield code="a">Renouard, Madalena</subfield>
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      <subfield code="a">Boulanger, Pascale</subfield>
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      <subfield code="a">van Raaij, Mark J</subfield>
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      <subfield code="c">2015-12-08</subfield>
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      <subfield code="a">Bacteriophage T5, a Siphovirus belonging to the order Caudovirales, has a flexible, three-fold symmetric tail, to which three L-shaped fibres are attached. These fibres recognize oligo-mannose units on the bacterial cell surface prior to infection and are composed of homotrimers of the pb1 protein. Pb1 has 1396 amino acids, of which the carboxy-terminal 133 residues form a trimeric intra-molecular chaperone that is auto-proteolyzed after correct folding. The structure of a trimer of residues 970-1263 was determined by single anomalous dispersion phasing using incorporated selenomethionine residues and refined at 2.3 Å resolution using crystals grown from native, methionine-containing, protein. The protein inhibits phage infection by competition. The phage-distal receptor-binding domain resembles a bullet, with the walls formed by partially intertwined beta-sheets, conferring stability to the structure. The fold of the domain is novel and the topology unique to the pb1 structure. A site-directed mutant (Ser1264 to Ala), in which auto-proteolysis is impeded, was also produced, crystallized and its 2.5 Å structure solved by molecular replacement. The additional chaperone domain (residues 1263-1396) consists of a central trimeric alpha-helical coiled-coil flanked by a mixed alpha-beta domain. Three long beta-hairpin tentacles, one from each chaperone monomer, extend into long curved grooves of the bullet-shaped domain. The chaperone-containing mutant did not inhibit infection by competition.</subfield>
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      <subfield code="a">Viruses. 2015 Dec 8;7(12):6424-40.</subfield>
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      <subfield code="a">10.3390/v7122946</subfield>
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      <subfield code="a">1999-4915</subfield>
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      <subfield code="a">Viruses</subfield>
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      <subfield code="a">26670244</subfield>
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      <subfield code="a">http://hdl.handle.net/20.500.12105/8974</subfield>
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      <subfield code="a">Caudovirales</subfield>
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      <subfield code="a">J0101</subfield>
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      <subfield code="a">Siphoviridae</subfield>
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      <subfield code="a">bacterial viruses</subfield>
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      <subfield code="a">crystallography</subfield>
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      <subfield code="a">infection</subfield>
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      <subfield code="a">Structure of the Receptor-Binding Carboxy-Terminal Domain of the Bacteriophage T5 L-Shaped Tail Fibre with and without Its Intra-Molecular Chaperone</subfield>
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