Another interest of my group are very high resolution (1.0 or better) structures of phosphate binding protein. These studies require synchrotron-generated X-rays of very high brilliance. Atomic structures at this resolution are able to reveal details of hydrogen bonding that cannot be obtained by other methods.

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Shown is a very short hydrogen bond between an Asp and a phosphate is established in two high resolution structures (0.98 and 1.05 A). A mutant complex that changes the Asp to an Asn, which forms a normal hydrogen bond, has a similar free energy of binding to the wild type complex, suggesting that the contribution of the short hydrogen bond is not extraordinarily strong.

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Also shown is Trp156 electron density, clearly showing the individual carbon bulges allowing for its unmistakable identification.

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Shown here is a tyrosine's electron density.

A low energy short hydrogen bond in very high resolution structures of protein receptor--phosphate complexes.Wang Z, Luecke H, Yao N, Quiocho FA (1997) Nat. Struct. Biol. 4(7):519-522 (abstract)

High specificity of a phosphate transport protein determined by hydrogen bonds. Luecke H, Quiocho FA (1990) Nature 347(6291):402-406 (abstract)

This page created 8/8/98 by JP, last modified 2/25/2000.