1gqt: Difference between revisions

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[[Category: transferase]]
[[Category: transferase]]


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Revision as of 16:12, 30 October 2007

File:1gqt.gif


1gqt, resolution 2.34Å

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ACTIVATION OF RIBOKINASE BY MONOVALENT CATIONS

OverviewOverview

Carbohydrate kinases frequently require a monovalent cation for their, activity. The physical basis of this phenomenon is, however, usually, unclear. We report here that Escherichia coli ribokinase is activated by, potassium with an apparent K(d) of 5 mM; the enzyme should therefore be, fully activated under physiological conditions. Cesium can be used as an, alternative ion, with an apparent K(d) of 17 mM. An X-ray structure of, ribokinase in the presence of cesium was solved and refined at 2.34 A, resolution. The cesium ion was bound between two loops immediately, adjacent to the anion hole of the active site. The buried location of the, site suggests that conformational changes will accompany ion binding, thus, providing a direct mechanism for activation. Comparison with structures of, ... [(full description)]

About this StructureAbout this Structure

1GQT is a [Single protein] structure of sequence from [Escherichia coli] with RIB, CS and ACP as [ligands]. Active as [Ribokinase], with EC number [2.7.1.15]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

ReferenceReference

Activation of ribokinase by monovalent cations., Andersson CE, Mowbray SL, J Mol Biol. 2002 Jan 18;315(3):409-19. PMID:11786021

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