PDBsum entry: 1hy8

Lipid binding protein

PDB id: 1hy8

Contents

Protein chain

76 a.a. *

* Residue conservation analysis

PDB id:

1hy8

Name:

Lipid binding protein

Title:

Solution structure of b. Subtilis acyl carrier protein

Structure:

Acyl carrier protein. Chain: a. Synonym: acp. Engineered: yes

Source:

Bacillus subtilis. Organism_taxid: 1423. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

NMR struc:

1 models

Authors:

G.-Y.Xu,A.Tam,L.Lin,J.Hixon,C.C.Fritz,R.Power

Key ref:

G.Y.Xu et al. (2001). Solution structure of B. subtilis acyl carrier protein. Structure, 9, 277-287. PubMed id: 11525165 DOI: 10.1016/S0969-2126(01)00586-X

Date:

18-Jan-01 Release date: 23-Jan-02

Protein chain

P80643  (ACP_BACSU) -  Acyl carrier protein

Seq: 77 a.a.

Struc: 76 a.a.

 Gene Ontology (GO) functional annotation 

• Cellular component: cytoplasm (1 term)
• Biological process: lipid biosynthetic process (2 terms)
• Biochemical function: cofactor binding (3 terms)

DOI no: 10.1016/S0969-2126(01)00586-X

Structure 9:277-287 (2001)

PubMed id: 11525165

Solution structure of B. subtilis acyl carrier protein.

G.Y.Xu, A.Tam, L.Lin, J.Hixon, C.C.Fritz, R.Powers.

ABSTRACT

BACKGROUND: Acyl carrier protein (ACP) is a fundamental component of fatty acid biosynthesis in which the fatty acid chain is elongated by the fatty acid synthetase system while attached to the 4'-phosphopantetheine prosthetic group (4'-PP) of ACP. Activation of ACP is mediated by holo-acyl carrier protein synthase (ACPS) when ACPS transfers the 4'-PP moiety from coenzyme A (CoA) to Ser36 of apo-ACP. Both ACP and ACPS have been identified as essential for E. coli viability and potential targets for development of antibiotics. RESULTS: The solution structure of B. subtilis ACP (9 kDa) has been determined using two-dimensional and three-dimensional heteronuclear NMR spectroscopy. A total of 22 structures were calculated by means of hybrid distance geometry-simulated annealing using a total of 1,050 experimental NMR restraints. The atomic rmsd about the mean coordinate positions for the 22 structures is 0.45 +/- 0.08 A for the backbone atoms and 0.93 +/- 0.07 A for all atoms. The overall ACP structure consists of a four alpha-helical bundle in which 4'-PP is attached to the conserved Ser36 that is located in alpha helix II. CONCLUSIONS: Structural data were collected for both the apo and holo forms of ACP that suggest that the two forms of ACP are essentially identical. Comparison of the published structures for E. coli ACP and actinorhodin polyketide synthase acyl carrier protein (act apo-ACP) from Streptomyces coelicolor A3(2) with B. subtilis ACP indicates similar secondary structure elements but an extremely large rmsd between the three ACP structures (>4.3 A). The structural difference between B. subtilis ACP and both E. coli and act apo-ACP is not attributed to an inherent difference in the proteins, but is probably a result of a limitation in the methodology available for the analysis for E. coli and act apo-ACP. Comparison of the structure of free ACP with the bound form of ACP in the ACP-ACPS complex reveals a displacement of helix II in the vicinity of Ser36. The induced perturbation of ACP by ACPS positions Ser36 proximal to coenzyme A and aligns the dipole of helix II to initiate transfer of 4'-PP to ACP.

Selected figure(s)

Figure 4.
Figure 4. Overlays of the Ribbon Diagrams of B. subtilis ACP with the E. coli, act apo, and X-ray ACP Structures(a) B. subtilis ACP (red) and E. coli ACP (green).(b) B. subtilis ACP (red) and act apo-ACP (blue).(c) Free ACP NMR (red) and X-ray ACP in the ACP-ACPS complex (turquoise)

The above figure is reprinted by permission from Cell Press: Structure (2001, 9, 277-287) copyright 2001.

Figure was selected by an automated process.