1v5x

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Revision as of 02:30, 25 November 2007

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spinqualitylabelsall models 1v5x, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Crystal structure of Phosphoribosyl anthranilate isomerase from Thermus Thermophilus

Overview

The crystal structure of phosphoribosyl anthranilate isomerase (PRAI) from, Thermus thermophilus HB8 (TtPRAI) was solved at 2.0 A resolution. The, overall structure of TtPRAI with a dimeric structure was quite similar to, that of PRAI from Thermotoga maritima (TmPRAI). In order to elucidate the, stabilization mechanism of TtPRAI, its physicochemical properties were, examined using DSC, CD, and analytical centrifugation at various pHs in, relation to the association-dissociation of the subunits. Based on the, experimental results for TtPRAI and the structural information on TtPRAI, and TmPRAI, we found that: (i) the denaturation of TtPRAI at acidic pH is, correlated with the dissociation of its dimeric form; (ii) the hydrophobic, interaction of TtPRAI in the monomer structure is slightly greater than, that of TmPRAI, but dimer interface of the TmPRAI is remarkably greater;, (iii) the contributions of hydrogen bonds and ion bonds to the stability, are similar to each other; and (iv) destabilization due to the presence of, cavities in TtPRAI is greater than that of TmPRAI in both the monomer and, dimer structures.

About this Structure

1V5X is a Single protein structure of sequence from Thermus thermophilus. Active as Phosphoribosylanthranilate isomerase, with EC number 5.3.1.24 Full crystallographic information is available from OCA.

Reference

Stabilization due to dimer formation of phosphoribosyl anthranilate isomerase from Thermus thermophilus HB8: X-ray Analysis and DSC experiments., Taka J, Ogasahara K, Jeyakanthan J, Kunishima N, Kuroishi C, Sugahara M, Yokoyama S, Yutani K, J Biochem (Tokyo). 2005 May;137(5):569-78. PMID:15944409

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