1gqt
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(New page: 200px<br /> <applet load="1gqt" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gqt, resolution 2.34Å" /> '''ACTIVATION OF RIBOK...)
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Revision as of 20:02, 29 October 2007
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ACTIVATION OF RIBOKINASE BY MONOVALENT CATIONS
Overview
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 Structure
1GQT is a [Single protein] structure of sequence from [Escherichia coli] with RIB, CS and ACP as [ligands]. Active as [[1]], with EC number [2.7.1.15]. Full crystallographic information is available from [OCA].
Reference
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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