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PDBsum entry 4owc
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Enzyme class:
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E.C.3.2.1.17
- lysozyme.
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Reaction:
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Hydrolysis of the 1,4-beta-linkages between N-acetyl-D-glucosamine and N-acetylmuramic acid in peptidoglycan heteropolymers of the prokaryotes cell walls.
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DOI no:
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Acta Crystallogr F Struct Biol Commun
70:1132-1134
(2014)
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PubMed id:
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The binding of platinum hexahalides (Cl, Br and I) to hen egg-white lysozyme and the chemical transformation of the PtI6 octahedral complex to a PtI3 moiety bound to His15.
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S.W.Tanley,
L.V.Starkey,
L.Lamplough,
S.Kaenket,
J.R.Helliwell.
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ABSTRACT
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This study examines the binding and chemical stability of the platinum
hexahalides K2PtCl6, K2PtBr6 and K2PtI6 when soaked into pre-grown hen egg-white
lysozyme (HEWL) crystals as the protein host. Direct comparison of the iodo
complex with the chloro and bromo complexes shows that the iodo complex is
partly chemically transformed to a square-planar PtI3 complex bound to the N(δ)
atom of His15, a chemical behaviour that is not exhibited by the chloro or bromo
complexes. Each complex does, however, bind to HEWL in its octahedral form
either at one site (PtI6) or at two sites (PtBr6 and PtCl6). As heavy-atom
derivatives of a protein, the octahedral shape of the hexahalides could be
helpful in cases of difficult-to-interpret electron-density maps as they would
be recognisable `objects'.
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');
}
}
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