1bx4
From Proteopedia
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| - | [[Image:1bx4.gif|left|200px]]<br /> | + | [[Image:1bx4.gif|left|200px]]<br /><applet load="1bx4" size="450" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1bx4" size="450" color="white" frame="true" align="right" spinBox="true" | + | |
caption="1bx4, resolution 1.50Å" /> | caption="1bx4, resolution 1.50Å" /> | ||
'''STRUCTURE OF HUMAN ADENOSINE KINASE AT 1.50 ANGSTROMS'''<br /> | '''STRUCTURE OF HUMAN ADENOSINE KINASE AT 1.50 ANGSTROMS'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1BX4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with CL, MG and ADN as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Adenosine_kinase Adenosine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.20 2.7.1.20] | + | 1BX4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with CL, MG and ADN as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Adenosine_kinase Adenosine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.20 2.7.1.20] Known structural/functional Sites: <scene name='pdbsite=ADA:Adn 350 Binds In The Substrate Binding Site'>ADA</scene> and <scene name='pdbsite=ADB:Adn 355 Binds In The Atp Binding Site'>ADB</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BX4 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: human adenosine kinase]] | [[Category: human adenosine kinase]] | ||
| - | ''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 14:35:13 2007'' |
Revision as of 12:25, 18 December 2007
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STRUCTURE OF HUMAN ADENOSINE KINASE AT 1.50 ANGSTROMS
Overview
Adenosine kinase (AK) is a key enzyme in the regulation of extracellular, adenosine and intracellular adenylate levels. Inhibitors of adenosine, kinase elevate adenosine to levels that activate nearby adenosine, receptors and produce a wide variety of therapeutically beneficial, activities. Accordingly, AK is a promising target for new analgesic, neuroprotective, and cardioprotective agents. We determined the structure, of human adenosine kinase by X-ray crystallography using MAD phasing, techniques and refined the structure to 1.5 A resolution. The enzyme, structure consisted of one large alpha/beta domain with nine beta-strands, eight alpha-helices, and one small alpha/beta-domain with five, beta-strands and two alpha-helices. The active site is formed along the, edge of the beta-sheet in the large domain while the small domain acts as, a lid to cover the upper face of the active site. The overall structure is, similar to the recently reported structure of ribokinase from Escherichia, coli [Sigrell et al. (1998) Structure 6, 183-193]. The structure of, ribokinase was determined at 1.8 A resolution and represents the first, structure of a new family of carbohydrate kinases. Two molecules of, adenosine were present in the AK crystal structure with one adenosine, molecule located in a site that matches the ribose site in ribokinase and, probably represents the substrate-binding site. The second adenosine site, overlaps the ADP site in ribokinase and probably represents the ATP site., A Mg2+ ion binding site is observed in a trough between the two adenosine, sites. The structure of the active site is consistent with the observed, substrate specificity. The active-site model suggests that Asp300 is an, important catalytic residue involved in the deprotonation of the, 5'-hydroxyl during the phosphate transfer.
About this Structure
1BX4 is a Single protein structure of sequence from Homo sapiens with CL, MG and ADN as ligands. Active as Adenosine kinase, with EC number 2.7.1.20 Known structural/functional Sites: and . Full crystallographic information is available from OCA.
Reference
Structure of human adenosine kinase at 1.5 A resolution., Mathews II, Erion MD, Ealick SE, Biochemistry. 1998 Nov 10;37(45):15607-20. PMID:9843365
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