1dek: Difference between revisions

Revision as of 22:54, 30 June 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1dek.png

Template:STRUCTURE 1dek

DEOXYNUCLEOSIDE MONOPHOSPHATE KINASE COMPLEXED WITH DEOXY-GMPDEOXYNUCLEOSIDE MONOPHOSPHATE KINASE COMPLEXED WITH DEOXY-GMP

Template:ABSTRACT PUBMED 8670851

About this StructureAbout this Structure

1DEK is a Single protein structure of sequence from Enterobacteria phage t4. Full crystallographic information is available from OCA.

ReferenceReference

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

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OCA

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-'''DEOXYNUCLEOSIDE MONOPHOSPHATE KINASE COMPLEXED WITH DEOXY-GMP'''
+===DEOXYNUCLEOSIDE MONOPHOSPHATE KINASE COMPLEXED WITH DEOXY-GMP===
-==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.
+The line below this paragraph, {{ABSTRACT_PUBMED_8670851}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 8670851 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_8670851}}
 ==About this Structure==
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 [[Category: Phosphotransferase]]
 [[Category: Transferase]]
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