2j4e

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[[Category: nucleotide metabolism]]
[[Category: nucleotide metabolism]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 13:45:43 2007''
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 17:23:54 2007''

Revision as of 15:19, 30 October 2007


2j4e, resolution 2.80Å

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THE ITP COMPLEX OF HUMAN INOSINE TRIPHOSPHATASE

Overview

Inosine triphosphatase (ITPA) is a ubiquitous key regulator of cellular, non-canonical nucleotide levels. It breaks down inosine and xanthine, nucleotides generated by deamination of purine bases. Its enzymatic action, prevents accumulation of ITP and reduces the risk of incorporation of, potentially mutagenic inosine nucleotides into nucleic acids. Here we, describe the crystal structure of human ITPA in complex with its prime, substrate ITP, as well as the apoenzyme at 2.8 and 1.1A, respectively., These structures show for the first time the site of substrate and Mg2+, coordination as well as the conformational changes accompanying substrate, binding in this class of enzymes. Enzyme substrate interactions induce an, extensive closure of the nucleotide binding grove, resulting in tight, ... [(full description)]

About this Structure

2J4E is a [Single protein] structure of sequence from [Homo sapiens] with MG, ITT, POP and IMP as [ligands]. Active as [Nucleoside-triphosphate diphosphatase], with EC number [3.6.1.19]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

Crystal structure of human inosine triphosphatase. Substrate binding and implication of the inosine triphosphatase deficiency mutation P32T., Stenmark P, Kursula P, Flodin S, Graslund S, Landry R, Nordlund P, Schuler H, J Biol Chem. 2007 Feb 2;282(5):3182-7. Epub 2006 Nov 29. PMID:17138556

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