1k26

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Structure of a Nudix Protein from Pyrobaculum aerophilum Solved by the Single Wavelength Anomolous Scattering Method

Overview

Nudix proteins, formerly called MutT homolog proteins, are a large family, of proteins that play an important role in reducing the accumulation of, potentially toxic compounds inside the cell. They hydrolyze a wide variety, of substrates that are mainly composed of a nucleoside diphosphate linked, to some other moiety X and thus are called Nudix hydrolases. Here, the, crystal structure of a Nudix hydrolase from the hyperthermophilic archaeon, Pyrobaculum aerophilum is reported. The structure was determined by the, single-wavelength anomalous scattering method with data collected at the, peak anomalous wavelength of an iridium-derivatized crystal. It reveals an, extensive dimer interface, with each subunit contributing two strands to, the beta-sheet of the other subunit. Individual subunits consist of a, mixed highly twisted and curved beta-sheet of 11 beta-strands and two, alpha-helices, forming an alpha-beta-alpha sandwich. The conserved Nudix, box signature motif, which contains the essential catalytic residues, is, located at the first alpha-helix and the beta-strand and loop preceding, it. The unusually short connections between secondary-structural elements, together with the dimer form of the structure, are likely to contribute to, the thermostability of the P. aerophilum Nudix protein.

About this Structure

1K26 is a Single protein structure of sequence from Pyrobaculum aerophilum with SO4, IR3, NI, GOL and ACY as ligands. Full crystallographic information is available from OCA.

Reference

Structure of a Nudix protein from Pyrobaculum aerophilum reveals a dimer with two intersubunit beta-sheets., Wang S, Mura C, Sawaya MR, Cascio D, Eisenberg D, Acta Crystallogr D Biol Crystallogr. 2002 Apr;58(Pt 4):571-8. Epub 2002, Mar 22. PMID:11914479

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