3GIT

Crystal structure of a truncated acetyl-CoA synthase

3GIT の概要

• エントリーDOI: 10.2210/pdb3git/pdb
• 関連するPDBエントリー: 1OAO
• 分子名称: Carbon monoxide dehydrogenase/acetyl-CoA synthase subunit alpha, IRON/SULFUR CLUSTER, ZINC ION, ... (7 entities in total)
• 機能のキーワード: acetyltransferase, carbon dioxide fixation, iron, iron-sulfur, metal-binding, nickel, transferase
• 由来する生物種: Moorella thermoacetica
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 292254.56

構造登録者

Volbeda, A.,Darnault, C.,Fontecilla-Camps, J.C. (登録日: 2009-03-06, 公開日: 2009-10-06, 最終更新日: 2023-11-01)

主引用文献

Volbeda, A.,Darnault, C.,Tan, X.,Lindahl, P.A.,Fontecilla-Camps, J.C.
Novel domain arrangement in the crystal structure of a truncated acetyl-CoA synthase from Moorella thermoacetica
Biochemistry, 48:7916-7926, 2009

PubMed Abstract: Ni-dependent acetyl-CoA synthase (ACS) and CO dehydrogenase (CODH) constitute the central enzyme complex of the Wood-Ljungdahl pathway of acetyl-CoA formation. The crystal structure of a recombinant bacterial ACS lacking the N-terminal domain that interacts with CODH shows a large reorganization of the remaining two globular domains, producing a narrow cleft of suitable size, shape, and nature to bind CoA. Sequence comparisons with homologous archaeal enzymes that naturally lack the N-terminal domain show that many amino acids lining this cleft are conserved. Besides the typical [4Fe-4S] center, the A-cluster contains only one proximal metal ion that, according to anomalous scattering data, is most likely Cu or Zn. Incorporation of a functional Ni(2)Fe(4)S(4) A-cluster would require only minor structural rearrangements. Using available structures, a plausible model of the interaction between CODH and the smaller ACS in archaeal multienzyme complexes is presented, along with a discussion of evolutionary relationships of the archaeal and bacterial enzymes.

PubMed: 19650626
DOI: 10.1021/bi9003952

実験手法

X-RAY DIFFRACTION (3 Å)