2yxo

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spinqualitylabelsall models 2yxo, resolution 1.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Histidinol Phosphate Phosphatase complexed with Sulfate

Overview

Monofunctional histidinol phosphate phosphatase from Thermus thermophilus, HB8, which catalyzes the dephosphorylation of l-histidinol phosphate, belongs to the PHP family, together with the PHP domain of bacterial DNA, polymerase III and family X DNA polymerase. We have determined the, structures of the complex with a sulfate ion, the complex with a phosphate, ion, and the unliganded form at 1.6, 2.1, and 1.8 A resolution, respectively. The enzyme exists as a tetramer, and the subunit consists of, a distorted (betaalpha)7 barrel with one linker and one C-terminal tail., Three metal sites located on the C-terminal side of the barrel are, occupied by Fe1, Fe2, and Zn ions, respectively, forming a trinuclear, metal center liganded by seven histidines, one aspartate, one glutamate, and one hydroxide with two Fe ions bridged by the hydroxide. In the, complexes, the sulfate or phosphate ion is coordinated to three metal, ions, resulting in octahedral, trigonal bipyramidal, and tetrahedral, geometries around the Fe1, Fe2, and Zn ions, respectively. The ligand, residues are derived from the four motifs that characterize the PHP family, and from two motifs conserved in histidinol phosphate phosphatases. The, (betaalpha)7 barrel and the metal cluster are closely related in nature, and architecture to the (betaalpha)8 barrel and the mononuclear or, dinuclear metal center in the amidohydrolase superfamily, respectively., The coordination behavior of the phosphate ion toward the metal center, supports the mechanism in which the bridging hydroxide makes a direct, attack on the substrate phosphate tridentately bound to the two Fe ions, and Zn ion to hydrolyze the phosphoester bond.

About this Structure

2YXO is a Single protein structure of sequence from Thermus thermophilus with , , and as ligands. Active as Histidinol-phosphatase, with EC number 3.1.3.15 Full crystallographic information is available from OCA.

Reference

Crystal Structure of Monofunctional Histidinol Phosphate Phosphatase from Thermus thermophilus HB8(double dagger)., Omi R, Goto M, Miyahara I, Manzoku M, Ebihara A, Hirotsu K, Biochemistry. 2007 Nov 6;46(44):12618-27. Epub 2007 Oct 11. PMID:17929834

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