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International Union of Crystallography, Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 12(65), p. 1218-1221, 2009

DOI: 10.1107/s1744309109046302

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Structure of a putative β-phosphoglucomutase (TM1254) fromThermotoga maritima

Journal article published in 2009 by Richard W. Strange, Svetlana V. Antonyuk ORCID, Mark J. Ellis, Yoshitaka Bessho, Seiki Kuramitsu, Akeo Shinkai, Shigeyuki Yokoyama, S. Samar Hasnain
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This paper is available in a repository.

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Abstract

The structure of TM1254, a putative beta-phosphoglucomutase from T. maritima, was determined to 1.74 A resolution in a high-throughput structural genomics programme. Diffraction data were obtained from crystals belonging to space group P22(1)2(1), with unit-cell parameters a = 48.16, b = 66.70, c = 83.80 A, and were refined to an R factor of 19.2%. The asymmetric unit contained one protein molecule which is comprised of two domains. Structural homologues were found from protein databases that confirmed a strong resemblance between TM1254 and members of the haloacid dehalogenase (HAD) hydrolase family.