2i5d
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(New page: 200px<br /> <applet load="2i5d" size="450" color="white" frame="true" align="right" spinBox="true" caption="2i5d, resolution 1.630Å" /> '''Crystal Structure ...)
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Revision as of 20:34, 12 November 2007
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Crystal Structure of Human Inosine Triphosphate Pyrophosphatase
Contents |
Overview
The structure of human inosine triphosphate pyrophosphohydrolase (ITPA), has been determined using diffraction data to 1.6 A resolution. ITPA, contributes to the accurate replication of DNA by cleansing cellular dNTP, pools of mutagenic nucleotide purine analogs such as dITP or dXTP. A, similar high-resolution unpublished structure has been deposited in the, Protein Data Bank from a monoclinic and pseudo-merohedrally twinned, crystal. Here, cocrystallization of ITPA with a molar ratio of XTP appears, to have improved the crystals by eliminating twinning and resulted in an, orthorhombic space group. However, there was no evidence for bound XTP in, the structure. Comparison with substrate-bound NTPase from a thermophilic, organism predicts the movement of residues within helix alpha1, the loop, before alpha6 and helix alpha7 to cap off the active site when substrate, is bound.
Disease
Known disease associated with this structure: Inosine triphosphatase deficiency OMIM:[147520]
About this Structure
2I5D is a Single protein structure of sequence from Homo sapiens. Active as Nucleoside-triphosphate diphosphatase, with EC number 3.6.1.19 Full crystallographic information is available from OCA.
Reference
Structure of the orthorhombic form of human inosine triphosphate pyrophosphatase., Porta J, Kolar C, Kozmin SG, Pavlov YI, Borgstahl GE, Acta Crystallograph Sect F Struct Biol Cryst Commun. 2006 Nov 1;62(Pt, 11):1076-81. Epub 2006 Oct 25. PMID:17077483
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