Literature DB >> 16511105

Crystallization and preliminary X-ray analysis of methylthioribose-1-phosphate isomerase from Bacillus subtilis.

Haruka Tamura1, Hiroyoshi Matsumura, Tsuyoshi Inoue, Hiroki Ashida, Yohtaro Saito, Akiho Yokota, Yasushi Kai.   

Abstract

Methylthioribose-1-phosphate isomerase (MtnA) from Bacillus subtilis, the first enzyme in the downstream section of the methionine-salvage pathway, was crystallized using the sitting-drop vapour-diffusion method. Crystals grew using ammonium sulfate as the precipitant at 293 K. They diffracted to 2.5 A at 100 K using synchrotron radiation and were found to belong to the tetragonal space group P4(1), with unit-cell parameters a = b = 69.2, c = 154.7 A. The asymmetric unit contains two molecules of MtnA, with a VM value of 2.4 A3 Da(-1) and a solvent content of 48%.

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Year:  2005        PMID: 16511105      PMCID: PMC1952323          DOI: 10.1107/S1744309105015757

Source DB:  PubMed          Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun        ISSN: 1744-3091


  19 in total

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  1 in total

1.  Crystal structure of 5-methylthioribose 1-phosphate isomerase product complex from Bacillus subtilis: implications for catalytic mechanism.

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