Structure of a putative beta-phosphoglucomutase (TM1254) from Thermotoga maritima.
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.
Strange
Richard W
RW
Molecular Biophysics Group, School of Biological Sciences, University of Liverpool, Crown Street, Liverpool L69 7ZB, England. r.strange@liverpool.ac.uk
Antonyuk
Svetlana V
SV
Ellis
Mark J
MJ
Bessho
Yoshitaka
Y
Kuramitsu
Seiki
S
Shinkai
Akeo
A
Yokoyama
Shigeyuki
S
Hasnain
S Samar
SS
D020134:Catalytic Domain; D003001:Cloning, Molecular; D018360:Crystallography, X-Ray; D005798:Genes, Bacterial; D008958:Models, Molecular; D010733:Phosphoglucomutase / Q000737:chemistry* / Q000235:genetics; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics; D040681:Structural Homology, Protein; D020124:Thermotoga maritima / Q000201:enzymology* / Q000235:genetics
D011994:Recombinant Proteins; D010733:Phosphoglucomutase