1del
From Proteopedia
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|PDB= 1del |SIZE=350|CAPTION= <scene name='initialview01'>1del</scene>, resolution 2.2Å | |PDB= 1del |SIZE=350|CAPTION= <scene name='initialview01'>1del</scene>, resolution 2.2Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=DGP:2'-DEOXYGUANOSINE-5'-MONOPHOSPHATE'>DGP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/(Deoxy)nucleoside-phosphate_kinase (Deoxy)nucleoside-phosphate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.4.13 2.7.4.13] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/(Deoxy)nucleoside-phosphate_kinase (Deoxy)nucleoside-phosphate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.4.13 2.7.4.13] </span> |
| - | |GENE= 1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id= | + | |GENE= 1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10665 Enterobacteria phage T4]) |
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1del FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1del OCA], [http://www.ebi.ac.uk/pdbsum/1del PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1del RCSB]</span> | ||
}} | }} | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1DEL is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ | + | 1DEL is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_t4 Enterobacteria phage t4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DEL OCA]. |
==Reference== | ==Reference== | ||
Crystal structure of bacteriophage T4 deoxynucleotide kinase with its substrates dGMP and ATP., Teplyakov A, Sebastiao P, Obmolova G, Perrakis A, Brush GS, Bessman MJ, Wilson KS, EMBO J. 1996 Jul 15;15(14):3487-97. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8670851 8670851] | Crystal structure of bacteriophage T4 deoxynucleotide kinase with its substrates dGMP and ATP., Teplyakov A, Sebastiao P, Obmolova G, Perrakis A, Brush GS, Bessman MJ, Wilson KS, EMBO J. 1996 Jul 15;15(14):3487-97. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8670851 8670851] | ||
[[Category: (Deoxy)nucleoside-phosphate kinase]] | [[Category: (Deoxy)nucleoside-phosphate kinase]] | ||
| - | [[Category: | + | [[Category: Enterobacteria phage t4]] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Sebastiao, P.]] | [[Category: Sebastiao, P.]] | ||
[[Category: Teplyakov, A.]] | [[Category: Teplyakov, A.]] | ||
| - | [[Category: AMP]] | ||
| - | [[Category: DGP]] | ||
| - | [[Category: MG]] | ||
[[Category: phosphotransferase]] | [[Category: phosphotransferase]] | ||
[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:40:06 2008'' |
Revision as of 16:40, 30 March 2008
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| , resolution 2.2Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Gene: | 1 (Enterobacteria phage T4) | ||||||
| Activity: | (Deoxy)nucleoside-phosphate kinase, with EC number 2.7.4.13 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
DEOXYNUCLEOSIDE MONOPHOSPHATE KINASE COMPLEXED WITH DEOXY-GMP AND AMP
Overview
NMP kinases catalyse the phosphorylation of the canonical nucleotides to the corresponding diphosphates using ATP as a phosphate donor. Bacteriophage T4 deoxynucleotide kinase (DNK) is the only member of this family of enzymes that recognizes three structurally dissimilar nucleotides: dGMP, dTMP and 5-hydroxymethyl-dCMP while excluding dCMP and dAMP. The crystal structure of DNK with its substrate dGMP has been determined at 2.0 A resolution by single isomorphous replacement. The structure of the ternary complex with dGMP and ATP has been determined at 2.2 A resolution. The polypeptide chain of DNK is folded into two domains of equal size, one of which resembles the mononucleotide binding motif with the glycine-rich P-loop. The second domain, consisting of five alpha-helices, forms the NMP binding pocket. A hinge connection between the domains allows for large movements upon substrate binding which are not restricted by dimerization of the enzyme. The mechanism of active centre formation via domain closure is described. Comparison with other P-loop-containing proteins indicates an induced-fit mode of NTP binding. Protein-substrate interactions observed at the NMP and NTP sites provide the basis for understanding the principles of nucleotide discrimination.
About this Structure
1DEL is a Single protein structure of sequence from Enterobacteria phage t4. Full crystallographic information is available from OCA.
Reference
Crystal structure of bacteriophage T4 deoxynucleotide kinase with its substrates dGMP and ATP., Teplyakov A, Sebastiao P, Obmolova G, Perrakis A, Brush GS, Bessman MJ, Wilson KS, EMBO J. 1996 Jul 15;15(14):3487-97. PMID:8670851
Page seeded by OCA on Sun Mar 30 19:40:06 2008
