PDBsum entry: 1l0i

Lipid transport

PDB id: 1l0i

Contents

Protein chain

77 a.a. *

Ligands

CAC

PSR

Metals

_NA

_ZN ×7

Waters ×162

* Residue conservation analysis

PDB id:

1l0i

Name:

Lipid transport

Title:

Crystal structure of butyryl-acp i62m mutant

Structure:

Acyl carrier protein. Chain: a. Synonym: acp, caf, cytosolic activating factor. Engineered: yes. Mutation: yes

Source:

Escherichia coli. Organism_taxid: 562. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

Resolution:

1.20Å R-factor: 0.160 R-free: 0.193

Authors:

A.Roujeinikova,C.Baldock,W.J.Simon,J.Gilroy,P.J.Baker,A.R.St D.W.Rice,A.R.Slabas,J.B.Rafferty

Key ref:

A.Roujeinikova et al. (2002). X-ray crystallographic studies on butyryl-ACP reveal flexibility of the structure around a putative acyl chain binding site. Structure, 10, 825-835. PubMed id: 12057197 DOI: 10.1016/S0969-2126(02)00775-X

Date:

11-Feb-02 Release date: 11-Feb-03

Protein chain

P0A6A8  (ACP_ECOLI) -  Acyl carrier protein

Seq: 78 a.a.

Struc: 77 a.a.*

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

 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(02)00775-X

Structure 10:825-835 (2002)

PubMed id: 12057197

X-ray crystallographic studies on butyryl-ACP reveal flexibility of the structure around a putative acyl chain binding site.

A.Roujeinikova, C.Baldock, W.J.Simon, J.Gilroy, P.J.Baker, A.R.Stuitje, D.W.Rice, A.R.Slabas, J.B.Rafferty.

ABSTRACT

Acyl carrier protein (ACP) is an essential cofactor in biosynthesis of fatty acids and many other reactions that require acyl transfer steps. We have determined the first crystal structures of an acylated form of ACP from E. coli, that of butyryl-ACP. Our analysis of the molecular surface of ACP reveals a plastic hydrophobic cavity in the vicinity of the phosphopantethylated Ser36 residue that is expanded and occupied by the butyryl and beta-mercaptoethylamine moieties of the acylated 4'-phosphopantetheine group in one of our crystal forms. In the other form, the cavity is contracted, and we propose that the protein has adopted the conformation after delivery of substrate into the active site of a partner enzyme.

Selected figure(s)

Figure 5.
Figure 5. Putative Binding Site for Acyl Chains(A) Solvent-accessible surface representation of the protein moiety of E. coli butyryl-ACP I62M. The surface is colored according to the electrostatic potential calculated with WebLabViewerPro4.0 (http://www.msi.com). The butyrylated prosthetic group, which was not included in the calculation of the surface, is shown in a stick representation and the disordered part of the molecule is represented by the dotted line.(B) A cross-section view showing the hydrophobic pocket that originates in the cleft flanked by helices a2 and a3. A butyryl group attached to the 4'-phosphopantetheine arm is presumed to occupy the pocket.(C) Stereo diagram showing residues that form a putative acyl chain binding site (same view as in [A] and [B]). The carbon atoms are colored gray in the protein and green in the bound ligand, nitrogen atoms are shown in blue, oxygen in red, and sulfur in yellow.

The above figure is reprinted by permission from Cell Press: Structure (2002, 10, 825-835) copyright 2002.

Figure was selected by the author.