2jas
From Proteopedia
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| - | [[Image:2jas.gif|left|200px]]<br /><applet load="2jas" size=" | + | [[Image:2jas.gif|left|200px]]<br /><applet load="2jas" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2jas, resolution 2.70Å" /> | caption="2jas, resolution 2.70Å" /> | ||
'''STRUCTURE OF DEOXYADENOSINE KINASE FROM M.MYCOIDES WITH BOUND DATP'''<br /> | '''STRUCTURE OF DEOXYADENOSINE KINASE FROM M.MYCOIDES WITH BOUND DATP'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2JAS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mycoplasma_mycoides_subsp._mycoides_sc Mycoplasma mycoides subsp. mycoides sc] with MG and DTP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Deoxyguanosine_kinase Deoxyguanosine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.113 2.7.1.113] Known structural/functional Site: <scene name='pdbsite=AC1:Dtp Binding Site For Chain F'>AC1</scene>. Full crystallographic information is available from [http:// | + | 2JAS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mycoplasma_mycoides_subsp._mycoides_sc Mycoplasma mycoides subsp. mycoides sc] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=DTP:'>DTP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Deoxyguanosine_kinase Deoxyguanosine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.113 2.7.1.113] Known structural/functional Site: <scene name='pdbsite=AC1:Dtp+Binding+Site+For+Chain+F'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JAS OCA]. |
==Reference== | ==Reference== | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 10:43:34 2008'' |
Revision as of 08:43, 3 February 2008
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STRUCTURE OF DEOXYADENOSINE KINASE FROM M.MYCOIDES WITH BOUND DATP
Overview
Deoxyribonucleoside kinases (dNKs) catalyze the transfer of a phosphoryl, group from ATP to a deoxyribonucleoside (dN), a key step in DNA precursor, synthesis. Recently structural information concerning dNKs has been, obtained, but no structure of a bacterial dCK/dGK enzyme is known. Here we, report the structure of such an enzyme, represented by deoxyadenosine, kinase from Mycoplasma mycoides subsp. mycoides small colony type, (Mm-dAK). Superposition of Mm-dAK with its human counterpart's, deoxyguanosine kinase (dGK) and deoxycytidine kinase (dCK) reveals that, the overall structures are very similar with a few amino acid alterations, in the proximity of the active site. To investigate the substrate, specificity, Mm-dAK has been crystallized in complex with dATP and dCTP, as well as the products dCMP and dCDP. Both dATP and dCTP bind to the, enzyme in a feedback-inhibitory manner with the dN part in the, deoxyribonucleoside binding site and the triphosphates in the P-loop., Substrate specificity studies with clinically important nucleoside analogs, as well as several phosphate donors were performed. Thus, in this study we, combine structural and kinetic data to gain a better understanding of the, substrate specificity of the dCK/dGK family of enzymes. The structure of, Mm-dAK provides a starting point for making new anti bacterial agents, against pathogenic bacteria.
About this Structure
2JAS is a Single protein structure of sequence from Mycoplasma mycoides subsp. mycoides sc with and as ligands. Active as Deoxyguanosine kinase, with EC number 2.7.1.113 Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
Structure-function analysis of a bacterial deoxyadenosine kinase reveals the basis for substrate specificity., Welin M, Wang L, Eriksson S, Eklund H, J Mol Biol. 2007 Mar 9;366(5):1615-23. Epub 2006 Dec 8. PMID:17229440
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