PDBsum entry 3git

Transferase

PDB id: 3git

Contents

Protein chains

(+ 0 more) 422 a.a. *

Ligands

SF4 ×6

H2S ×6

SO4 ×24

GOL ×6

Metals

_ZN ×6

Waters ×189

* Residue conservation analysis

PDB id:

3git

Name:

Transferase

Title:

Crystal structure of a truncated acetyl-coa synthase

Structure:

Carbon monoxide dehydrogenase/acetyl-coa synthase subunit alpha. Chain: a, b, c, d, e, f. Fragment: truncated domain, residues 311-729. Synonym: codh/acs, acetyl-coa synthase subunit, acs subunit. Engineered: yes

Source:

Moorella thermoacetica. Organism_taxid: 1525. Gene: acsb2. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

Resolution:

3.00Å R-factor: 0.173 R-free: 0.208

Authors:

A.Volbeda,C.Darnault,J.C.Fontecilla-Camps

Key ref:

A.Volbeda et al. (2009). Novel domain arrangement in the crystal structure of a truncated acetyl-CoA synthase from Moorella thermoacetica. Biochemistry, 48, 7916-7926. PubMed id: 19650626

Date:

06-Mar-09 Release date: 06-Oct-09

Protein chains

P27988  (DCMA_MOOTH) -  Carbon monoxide dehydrogenase/acetyl-CoA synthase subunit alpha from Moorella thermoacetica

Seq: 729 a.a.

Struc: 422 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

Enzyme reactions

• Enzyme class: E.C.2.3.1.169 - CO-methylating acetyl-CoA synthase.
• Reaction: Co(I)-[corrinoid Fe-S protein] + acetyl-CoA + H⁺ = methyl-Co(III)- [corrinoid Fe-S protein] + CO + CoA
• Cofactor: Cu(2+); Iron-sulfur; Ni(2+)

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

Biochemistry 48:7916-7926 (2009)

PubMed id: 19650626

Novel domain arrangement in the crystal structure of a truncated acetyl-CoA synthase from Moorella thermoacetica.

A.Volbeda, C.Darnault, X.Tan, P.A.Lindahl, J.C.Fontecilla-Camps.

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.