| Literature DB >> 20054115 |
Richard W Strange1, Svetlana V Antonyuk, Mark J Ellis, Yoshitaka Bessho, Seiki Kuramitsu, Akeo Shinkai, Shigeyuki Yokoyama, S Samar Hasnain.
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.Entities:
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Year: 2009 PMID： 20054115 PMCID： PMC2802867 DOI： 10.1107/S1744309109046302
Source DB: PubMed Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun ISSN： 1744-3091