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Structure of a putative beta-phosphoglucomutase (TM1254) from Thermotoga maritima.

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.

SUBMITTER: Strange RW

PROVIDER: S-EPMC2802867 | biostudies-literature | 2009 Dec

REPOSITORIES: biostudies-literature

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Structure of a putative beta-phosphoglucomutase (TM1254) from Thermotoga maritima.

Strange Richard W RW Antonyuk Svetlana V SV Ellis Mark J MJ Bessho Yoshitaka Y Kuramitsu Seiki S Shinkai Akeo A Yokoyama Shigeyuki S Hasnain S Samar SS

Acta crystallographica. Section F, Structural biology and crystallization communications 20091127 Pt 12

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 co ...[more]

PMID: 20054115

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Project description:This SuperSeries is composed of the SubSeries listed below.

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