PDBsum entry: 2hjw

Ligase

PDB id: 2hjw

Contents

Protein chain

494 a.a. *

Waters ×87

* Residue conservation analysis

PDB id:

2hjw

Name:

Ligase

Title:

Crystal structure of the bc domain of acc2

Structure:

Acetyl-coa carboxylase 2. Chain: a. Fragment: bc domain, residues 217-775. Synonym: acc2. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: acacb. Expressed in: escherichia coli bl21. Expression_system_taxid: 511693.

Resolution:

2.50Å R-factor: 0.212 R-free: 0.248

Authors:

Y.S.Cho,J.I.Lee,D.Shin,H.T.Kim,T.G.Lee,Y.S.Heo

Key ref:

Y.S.Cho et al. (2008). Crystal structure of the biotin carboxylase domain of human acetyl-CoA carboxylase 2. Proteins, 70, 268-272. PubMed id: 17876819 DOI: 10.1002/prot.21611

Date:

02-Jul-06 Release date: 03-Jul-07

Protein chain

O00763  (ACACB_HUMAN) -  Acetyl-CoA carboxylase 2

Seq: 2458 a.a.

Struc: 494 a.a.

Enzyme reactions

• Enzyme class 1: E.C.6.3.4.14 - Biotin carboxylase.
• Reaction: ATP + biotin-[carboxyl-carrier-protein] + CO₂ = ADP + phosphate + carboxy-biotin-[carboxyl-carrier-protein]
• Enzyme class 2: E.C.6.4.1.2 - Acetyl-CoA carboxylase.
• Reaction: ATP + acetyl-CoA + HCO₃^- = ADP + phosphate + malonyl-CoA
• Cofactor: Biotin

Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.

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

 Gene Ontology (GO) functional annotation 

• Biological process: metabolic process (1 term)
• Biochemical function: catalytic activity (4 terms)

reference

DOI no: 10.1002/prot.21611

Proteins 70:268-272 (2008)

PubMed id: 17876819

Crystal structure of the biotin carboxylase domain of human acetyl-CoA carboxylase 2.

Y.S.Cho, J.I.Lee, D.Shin, H.T.Kim, Y.H.Cheon, C.I.Seo, Y.E.Kim, Y.L.Hyun, Y.S.Lee, K.Sugiyama, S.Y.Park, S.Ro, J.M.Cho, T.G.Lee, Y.S.Heo.

ABSTRACT

No abstract given.

Selected figure(s)

Figure 1.
Figure 1. Structure of the BC domain of human ACC2. (A) The BC domain is shown in a ribbon model and the disordered regions (residues, 217-219, 225-238, 412-417, 657-665, and 687-698) shown as dotted lines. The disordered Ser222 is labeled. The four domains are colored individually. The N- and C-terminal regions are also indicated. (B) Structural comparison between the soraphen A binding site of human BC domain without soraphen A (purple) and that of yeast BC in complex with soraphen A (green). (C) Structural comparison between the BC domains from human ACC2 (purple) and yeast ACC (green), when the A- and C-domains of the two proteins are superimposed. To emphasize the structural differences, the B-domain, AB linker, and N-terminus are colored more strongly and labeled. The arrow indicates the putative ATP-binding site. (D) Sequence alignment of the BC domains of human ACC2, ACC1, rat ACC2, and yeast ACC. Conserved residues are shown in red. The serine residues of mammalian ACCs that are phosphorylated by AMPK are shown in green. The disordered residues of the N-terminus in the structure of the human ACC2 BC domain are indicated by a yellow box.

The above figure is reprinted by permission from John Wiley & Sons, Inc.: Proteins (2008, 70, 268-272) copyright 2008.