The host-binding domain of the P2 phage tail spike reveals a trimeric iron-binding structure
The adsorption and infection of bacteriophage P2 is mediated by tail fibres and tail spikes. The tail spikes on the tail baseplate are used to irreversibly adsorb to the host cells. Recently, a P2 phage tail‐spike protein, gpV, was purified and it was shown that a C‐terminal domain, Ser87–Leu211, is...
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Veröffentlicht in: | Acta crystallographica. Section F, Structural biology and crystallization communications Structural biology and crystallization communications, 2011-08, Vol.67 (8), p.837-841 |
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creator | Yamashita, Eiki Nakagawa, Atsushi Takahashi, Junichi Tsunoda, Kin-ichi Yamada, Seiko Takeda, Shigeki |
description | The adsorption and infection of bacteriophage P2 is mediated by tail fibres and tail spikes. The tail spikes on the tail baseplate are used to irreversibly adsorb to the host cells. Recently, a P2 phage tail‐spike protein, gpV, was purified and it was shown that a C‐terminal domain, Ser87–Leu211, is sufficient for the binding of gpV to host Escherichia coli membranes [Kageyama et al. (2009), Biochemistry, 48, 10129–10135]. In this paper, the crystal structure of the C‐terminal domain of P2 gpV is reported. The structure is a triangular pyramid and looks like a spearhead composed of an intertwined β‐sheet, a triple β‐helix and a metal‐binding region containing iron, calcium and chloride ions. |
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Section F, Structural biology and crystallization communications</title><addtitle>Acta Cryst. F</addtitle><description>The adsorption and infection of bacteriophage P2 is mediated by tail fibres and tail spikes. The tail spikes on the tail baseplate are used to irreversibly adsorb to the host cells. Recently, a P2 phage tail‐spike protein, gpV, was purified and it was shown that a C‐terminal domain, Ser87–Leu211, is sufficient for the binding of gpV to host Escherichia coli membranes [Kageyama et al. (2009), Biochemistry, 48, 10129–10135]. In this paper, the crystal structure of the C‐terminal domain of P2 gpV is reported. The structure is a triangular pyramid and looks like a spearhead composed of an intertwined β‐sheet, a triple β‐helix and a metal‐binding region containing iron, calcium and chloride ions.</description><subject>Amino Acid Sequence</subject><subject>Bacteriology</subject><subject>bacteriophage P2</subject><subject>Bacteriophage P2 - chemistry</subject><subject>Bacteriophage P2 - metabolism</subject><subject>Crystal structure</subject><subject>Crystallography, X-Ray</subject><subject>E coli</subject><subject>Escherichia coli</subject><subject>Escherichia coli - chemistry</subject><subject>Fibers</subject><subject>gpV</subject><subject>Iron - chemistry</subject><subject>Models, Molecular</subject><subject>Protein Binding</subject><subject>Protein Structure, Quaternary</subject><subject>Structural Communications</subject><subject>tail-spike proteins</subject><subject>Viral Tail Proteins - chemistry</subject><subject>Viral Tail Proteins - metabolism</subject><issn>1744-3091</issn><issn>1744-3091</issn><issn>2053-230X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2011</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFUV1rFDEUDaLYuvoDfJGADz6N5mPyMS9Cd3GrtGjBFRGEkM3c2U07O1mTTLX_3ixbl6oPhUCSe8853HsOQs8peU0pUW8-U1XXnDS0_IhomuYBOt6Vql3t4Z33EXqS0iUhnDdSP0ZHjOpylD5G3xdrwOuQcrX0Q-uHFW7DxvoBhw7n0rpgeLu2K8DZ-h6nrb8CHOEabJ-wxTn6DUTvsI9hOCikHEeXxwhP0aOuAOHZ7T1BX-bvFrP31fmn0w-zk_PKSUnqinWaa-mUXlImNKWSOCXFErhoNVdCSd44K8rIsoMWCCNdR1tKheJcKFCMT9Dbve52XG6gdTDkaHuzLdPZeGOC9ebvzuDXZhWuDaeieEeLwKtbgRh-jJCy2fjkoO_tAGFMpmFyZ2Mt7kVqzTktvquCfPkP8jKMcSg-GKp4WZKpEsgE0T3KxZBShO4wNSVmF7L5L-TCeXF33QPjT6oF0OwBP30PN_crmpNvc7aYCsLrwq32XJ8y_DpwbbwyUpU0zNePp2Z2trg4m7KpmfPfdEK_kQ</recordid><startdate>201108</startdate><enddate>201108</enddate><creator>Yamashita, Eiki</creator><creator>Nakagawa, Atsushi</creator><creator>Takahashi, Junichi</creator><creator>Tsunoda, Kin-ichi</creator><creator>Yamada, Seiko</creator><creator>Takeda, Shigeki</creator><general>International Union of Crystallography</general><general>Wiley Subscription Services, Inc</general><scope>BSCLL</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>7T7</scope><scope>7TM</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>201108</creationdate><title>The host-binding domain of the P2 phage tail spike reveals a trimeric iron-binding structure</title><author>Yamashita, Eiki ; 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subjects | Amino Acid Sequence Bacteriology bacteriophage P2 Bacteriophage P2 - chemistry Bacteriophage P2 - metabolism Crystal structure Crystallography, X-Ray E coli Escherichia coli Escherichia coli - chemistry Fibers gpV Iron - chemistry Models, Molecular Protein Binding Protein Structure, Quaternary Structural Communications tail-spike proteins Viral Tail Proteins - chemistry Viral Tail Proteins - metabolism |
title | The host-binding domain of the P2 phage tail spike reveals a trimeric iron-binding structure |
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