Abstract
The crystal structure of recombinant TroA, a zinc-binding protein component of an ATP-binding cassette transport system in Treponema pallidum, was determined at a resolution of 1.8 A. The organization of the protein is largely similar to other periplasmic ligand-binding proteins (PLBP), in that two independent globular domains interact with each other to create a zinc-binding cleft between them. The structure has one bound zinc pentavalently coordinated to residues from both domains. Unlike previous PLBP structures that have an interdomain hinge composed of beta-strands, the N- and C-domains of TroA are linked by a single long backbone helix. This unique backbone helical conformation was possibly adopted to limit the hinge motion associated with ligand exchange.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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ATP-Binding Cassette Transporters / chemistry*
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ATP-Binding Cassette Transporters / physiology
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Bacterial Proteins / chemistry
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Binding Sites
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Carrier Proteins / chemistry
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Escherichia coli Proteins*
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Models, Molecular
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Molecular Sequence Data
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Periplasm / chemistry*
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Periplasmic Binding Proteins*
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Photosynthetic Reaction Center Complex Proteins / chemistry
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Photosystem I Protein Complex*
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Protein Structure, Secondary
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Treponema pallidum / chemistry*
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X-Ray Diffraction
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Zinc / metabolism*
Substances
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ATP-Binding Cassette Transporters
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Bacterial Proteins
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Carrier Proteins
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Escherichia coli Proteins
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MalE protein, E coli
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PSI-A protein, Synechococcus
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Periplasmic Binding Proteins
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Photosynthetic Reaction Center Complex Proteins
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Photosystem I Protein Complex
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TroA protein, Treponema pallidum
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Zinc