2jaq: Difference between revisions
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'''STRUCTURE OF DEOXYADENOSINE KINASE FROM M. MYCOIDES WITH BOUND DCTP''' | {{Structure | ||
|PDB= 2jaq |SIZE=350|CAPTION= <scene name='initialview01'>2jaq</scene>, resolution 2.30Å | |||
|SITE= <scene name='pdbsite=AC1:Dcp+Binding+Site+For+Chain+B'>AC1</scene> | |||
|LIGAND= <scene name='pdbligand=DCP:2'-DEOXYCYTIDINE-5'-TRIPHOSPHATE'>DCP</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''STRUCTURE OF DEOXYADENOSINE KINASE FROM M. MYCOIDES WITH BOUND DCTP''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2JAQ is a [ | 2JAQ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mycoplasma_mycoides_subsp._mycoides_sc Mycoplasma mycoides subsp. mycoides sc]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JAQ OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/17229440 17229440] | ||
[[Category: Mycoplasma mycoides subsp. mycoides sc]] | [[Category: Mycoplasma mycoides subsp. mycoides sc]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:39:29 2008'' | ||
Revision as of 15:39, 20 March 2008
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| 2jaq, resolution 2.30Å | |||||||||||||
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| Sites: | AC1 | ||||||||||||
| Ligands: | DCP | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
STRUCTURE OF DEOXYADENOSINE KINASE FROM M. MYCOIDES WITH BOUND DCTP
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
2JAQ is a Single protein structure of sequence from Mycoplasma mycoides subsp. mycoides sc. 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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