2j4e
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THE ITP COMPLEX OF HUMAN INOSINE TRIPHOSPHATASE
OverviewOverview
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 StructureAbout 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].
ReferenceReference
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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- Homo sapiens
- Nucleoside-triphosphate diphosphatase
- Single protein
- Arrowsmith, C.
- Berg, S.Van.Den.
- Berglund, H.
- Busam, R.
- Collins, R.
- Edwards, A.
- Ehn, M.
- Flodin, S.
- Flores, A.
- Graslund, S.
- Hallberg, B.M.
- Hammarstrom, M.
- Hogbom, M.
- Kotenyova, T.
- Kursula, P.
- Landry, R.
- Loppnau, P.
- Magnusdottir, A.
- Nilsson-Ehle, P.
- Nordlund, P.
- Nyman, T.
- Ogg, D.
- Persson, C.
- Sagemark, J.
- Schiavone, L.Holmberg.
- Schuler, H.
- Stenmark, P.
- Sundstrom, M.
- Thorsell, A.G.
- Uppenberg, J.
- Wallden, K.
- Weigelt, J.
- IMP
- ITT
- MG
- POP
- Disease mutation
- Hydrolase
- Imp
- Inosine triphosphatase deficiency
- Inosine triphosphate pyrophosphohydrolase
- Itp
- Nucleotide metabolism