2ocp
From Proteopedia
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|PDB= 2ocp |SIZE=350|CAPTION= <scene name='initialview01'>2ocp</scene>, resolution 2.80Å | |PDB= 2ocp |SIZE=350|CAPTION= <scene name='initialview01'>2ocp</scene>, resolution 2.80Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=DTP:2'-DEOXYADENOSINE 5'-TRIPHOSPHATE'>DTP</scene> | + | |LIGAND= <scene name='pdbligand=DTP:2'-DEOXYADENOSINE+5'-TRIPHOSPHATE'>DTP</scene> |
| - | |ACTIVITY= [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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= DGUOK, DGK ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |GENE= DGUOK, DGK ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1jag|1JAG]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ocp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ocp OCA], [http://www.ebi.ac.uk/pdbsum/2ocp PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2ocp RCSB]</span> | ||
}} | }} | ||
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==Overview== | ==Overview== | ||
Deoxyribonucleoside kinases phosphorylate deoxyribonucleosides and activate a number of medically important nucleoside analogs. Here we report the structure of the Drosophila deoxyribonucleoside kinase with deoxycytidine bound at the nucleoside binding site and that of the human deoxyguanosine kinase with ATP at the nucleoside substrate binding site. Compared to the human kinase, the Drosophila kinase has a wider substrate cleft, which may be responsible for the broad substrate specificity of this enzyme. The human deoxyguanosine kinase is highly specific for purine substrates; this is apparently due to the presence of Arg 118, which provides favorable hydrogen bonding interactions with the substrate. The two new structures provide an explanation for the substrate specificity of cellular deoxyribonucleoside kinases. | Deoxyribonucleoside kinases phosphorylate deoxyribonucleosides and activate a number of medically important nucleoside analogs. Here we report the structure of the Drosophila deoxyribonucleoside kinase with deoxycytidine bound at the nucleoside binding site and that of the human deoxyguanosine kinase with ATP at the nucleoside substrate binding site. Compared to the human kinase, the Drosophila kinase has a wider substrate cleft, which may be responsible for the broad substrate specificity of this enzyme. The human deoxyguanosine kinase is highly specific for purine substrates; this is apparently due to the presence of Arg 118, which provides favorable hydrogen bonding interactions with the substrate. The two new structures provide an explanation for the substrate specificity of cellular deoxyribonucleoside kinases. | ||
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| - | ==Disease== | ||
| - | Known diseases associated with this structure: Mitochondrial DNA-depletion syndrome, hepatocerebral form OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=601465 601465]] | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Piskur, J.]] | [[Category: Piskur, J.]] | ||
[[Category: Ramaswamy, S.]] | [[Category: Ramaswamy, S.]] | ||
| - | [[Category: DTP]] | ||
[[Category: protein-nucleotide complex]] | [[Category: protein-nucleotide complex]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:15:55 2008'' |
Revision as of 01:16, 31 March 2008
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| , resolution 2.80Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | DGUOK, DGK (Homo sapiens) | ||||||
| Activity: | Deoxyguanosine kinase, with EC number 2.7.1.113 | ||||||
| Related: | 1JAG
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of Human Deoxyguanosine Kinase
Overview
Deoxyribonucleoside kinases phosphorylate deoxyribonucleosides and activate a number of medically important nucleoside analogs. Here we report the structure of the Drosophila deoxyribonucleoside kinase with deoxycytidine bound at the nucleoside binding site and that of the human deoxyguanosine kinase with ATP at the nucleoside substrate binding site. Compared to the human kinase, the Drosophila kinase has a wider substrate cleft, which may be responsible for the broad substrate specificity of this enzyme. The human deoxyguanosine kinase is highly specific for purine substrates; this is apparently due to the presence of Arg 118, which provides favorable hydrogen bonding interactions with the substrate. The two new structures provide an explanation for the substrate specificity of cellular deoxyribonucleoside kinases.
About this Structure
2OCP is a Single protein structure of sequence from Homo sapiens. This structure supersedes the now removed PDB entry 1JAG. Full crystallographic information is available from OCA.
Reference
Structural basis for substrate specificities of cellular deoxyribonucleoside kinases., Johansson K, Ramaswamy S, Ljungcrantz C, Knecht W, Piskur J, Munch-Petersen B, Eriksson S, Eklund H, Nat Struct Biol. 2001 Jul;8(7):616-20. PMID:11427893
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