1NOG

Crystal Structure of Conserved Protein 0546 from Thermoplasma Acidophilum

1NOG の概要

• エントリーDOI: 10.2210/pdb1nog/pdb
• 分子名称: conserved hypothetical protein TA0546 (2 entities in total)
• 機能のキーワード: structural genomics, psi, protein structure initiative, midwest center for structural genomics, mcsg, unknown function
• 由来する生物種: Thermoplasma acidophilum
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 20029.07

構造登録者

Saridakis, V.,Sanishvili, R.,Iakounine, A.,Xu, X.,Pennycooke, M.,Gu, J.,Joachimiak, A.,Arrowsmith, C.H.,Edwards, A.M.,Christendat, D.,Midwest Center for Structural Genomics (MCSG) (登録日: 2003-01-16, 公開日: 2003-07-29, 最終更新日: 2024-02-14)

主引用文献

Saridakis, V.,Yakunin, A.,Xu, X.,Anandakumar, P.,Pennycooke, M.,Gu, J.,Cheung, F.,Lew, J.M.,Sanishvili, R.,Joachimiak, A.,Arrowsmith, C.H.,Christendat, D.,Edwards, A.M.
The structural basis for methylmalonic aciduria. The crystal structure of archaeal ATP:cobalamin adenosyltransferase.
J.Biol.Chem., 279:23646-23653, 2004

PubMed Abstract: ATP:cobalamin adenosyltransferase MMAB was recently identified as the gene responsible for a disorder of cobalamin metabolism in humans (cblB complementation group). The crystal structure of the MMAB sequence homologue from Thermoplasma acidophilum (TA1434; GenBank identification number gi|16082403) was determined to a resolution of 1.5 A. TA1434 was confirmed to be an ATP:cobalamin adenosyltransferase, which depended absolutely on divalent metal ions (Mg2+ > Mn2+ > Co2+) and only used ATP or dATP as adenosyl donors. The apparent Km of TA1434 was 110 microM (kcat = 0.23 s(-1)) for ATP, 140 microM (kcat = 0.11 s(-1)) for dATP, and 3 microM (kcat = 0.18 s(-1)) for cobalamin. TA1434 is a trimer in solution and in the crystal structure, with each subunit composed of a five-helix bundle. The location of disease-related point mutations and other residues conserved among the homologues of TA1434 suggest that the active site lies at the junctions between the subunits. Mutations in TA1434 that correspond to the disease-related mutations resulted in proteins that were inactive for ATP:cobalamin adenosyltransferase activity in vitro, confirming that these mutations define the molecular basis of the human disease.

PubMed: 15044458
DOI: 10.1074/jbc.M401395200

実験手法

X-RAY DIFFRACTION (1.55 Å)