1gqt
From Proteopedia
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| - | [[Image:1gqt. | + | [[Image:1gqt.jpg|left|200px]]<br /><applet load="1gqt" size="450" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1gqt" size="450" color="white" frame="true" align="right" spinBox="true" | + | |
caption="1gqt, resolution 2.34Å" /> | caption="1gqt, resolution 2.34Å" /> | ||
'''ACTIVATION OF RIBOKINASE BY MONOVALENT CATIONS'''<br /> | '''ACTIVATION OF RIBOKINASE BY MONOVALENT CATIONS'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1GQT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with RIB, CS and ACP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Ribokinase Ribokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.15 2.7.1.15] | + | 1GQT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with RIB, CS and ACP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Ribokinase Ribokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.15 2.7.1.15] Known structural/functional Site: <scene name='pdbsite=AC1:Rib Binding Site For Chain D'>AC1</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GQT OCA]. |
==Reference== | ==Reference== | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 15:31:47 2007'' |
Revision as of 13:22, 18 December 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, a related enzyme, the adenosine kinase of Toxoplasma gondii, support this, proposal. This is apparently the first instance in which conformational, activation of a carbohydrate kinase by a monovalent cation has been, assigned a clear structural basis. The mechanism is probably general to, ribokinases, to some adenosine kinases, and to other members of the larger, family. A careful re-evaluation of the biochemical and structural data is, suggested for other enzyme systems.
About 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 Known structural/functional Site: . 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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