3KBB

Crystal structure of putative beta-phosphoglucomutase from Thermotoga maritima

Replaces:  2PIB

Summary for 3KBB

• Entry DOI: 10.2210/pdb3kbb/pdb
• Descriptor: Phosphorylated carbohydrates phosphatase TM_1254, SULFATE ION, GLYCEROL, ... (4 entities in total)
• Functional Keywords: hydrolase, arbohydrate metabolism, thermotoga maritima, cobalt, magnesium, manganese, metal-binding, nickel, nppsfa, national project on protein structural and functional analyses, riken structural genomics/proteomics initiative, rsgi
• Biological source: Thermotoga maritima msb8
• Total number of polymer chains: 1
• Total formula weight: 25699.60

Authors

Strange, R.W.,Antonyuk, S.V.,Ellis, M.J.,Bessho, Y.,Kuramitsu, S.,Yokoyama, S.,Hasnain, S.S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2009-10-20, release date: 2009-11-17, Last modification date: 2024-10-09)

Primary citation

Strange, R.W.,Antonyuk, S.V.,Ellis, M.J.,Bessho, Y.,Kuramitsu, S.,Shinkai, A.,Yokoyama, S.,Hasnain, S.S.
Structure of a putative beta-phosphoglucomutase (TM1254) from Thermotoga maritima.
Acta Crystallogr.,Sect.F, 65:1218-1221, 2009

PubMed 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.

PubMed: 20054115
DOI: 10.1107/S1744309109046302

Experimental method

X-RAY DIFFRACTION (1.74 Å)