PDBsum entry 2afd

Ligand binding protein

PDB id: 2afd

Contents

Protein chain

88 a.a. *

* Residue conservation analysis

PDB id:

2afd

Name:

Ligand binding protein

Title:

Solution structure of asl1650, an acyl carrier protein from anabaena sp. Pcc 7120 with a variant phosphopantetheinylation-site sequence

Structure:

Protein asl1650. Chain: a. Engineered: yes. Mutation: yes

Source:

Nostoc sp.. Organism_taxid: 103690. Strain: pcc 7120. Expressed in: escherichia coli. Expression_system_taxid: 562. Other_details: synonym nostoc sp. Pcc 7120

NMR struc:

20 models

Authors:

M.A.Johnson,W.Peti,T.Herrmann,I.A.Wilson,K.Wuthrich,Joint Center For Structural Genomics (Jcsg)

Key ref:

M.A.Johnson et al. (2006). Solution structure of Asl1650, an acyl carrier protein from Anabaena sp. PCC 7120 with a variant phosphopantetheinylation-site sequence. Protein Sci, 15, 1030-1041. PubMed id: 16597827 DOI: 10.1110/ps.051964606

Date:

25-Jul-05 Release date: 16-Aug-05

Protein chain

Q8YWG3  (Q8YWG3_NOSS1) -  Asl1650 protein from Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)

Seq: 85 a.a.

Struc: 88 a.a.*

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

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1110/ps.051964606

Protein Sci 15:1030-1041 (2006)

PubMed id: 16597827

Solution structure of Asl1650, an acyl carrier protein from Anabaena sp. PCC 7120 with a variant phosphopantetheinylation-site sequence.

M.A.Johnson, W.Peti, T.Herrmann, I.A.Wilson, K.Wüthrich.

ABSTRACT

Cyanobacteria, such as Anabaena, produce a variety of bioactive natural products via polyketide synthases (PKS), nonribosomal peptide synthetases (NRPS), and hybrid peptide/polyketide pathways. The protein Asl1650, which is a member of the acyl carrier protein family from the cyanobacterium Anabaena sp. PCC 7120, is encoded in a region of the Anabaena genome that is rich in PKS and NRPS genes. To gain new insight into the physiological role of acyl carriers in Anabaena, the solution structure of Asl1650 has been solved by NMR spectroscopy. The protein adopts a twisted antiparallel four-helix bundle fold, with a variant phosphopantetheine-attachment motif positioned at the start of the second helix. Structure comparisons with proteins from other organisms suggest a likely physiological function as a discrete peptidyl carrier protein.

Selected figure(s)

Figure 2.
Wall-eye stereo views of the NMR structure of the protein Asl1650. (A) Bundle of 20 energy-minimized DYANA conformers. (Blue) Polypeptide backbone, (gold) hydrophobic side chains of the protein core. The positions of selected hydrophobic core residues are identified with the sequence numbers. (B) Ribbon diagram of the Asl1650 conformer with the lowest RMSD to the mean coordinates of the bundle of 20 conformers in panel A. The four helices forming a helix bundle (see text) are labeled [alpha]I, [alpha]II, 3[10](III), and [alpha]IV at their N termini. The chain-terminal residues [minus sign]3 and 85 are indicated.

Figure 4.
Wall-eye stereo view illustrating structural similarity in the region of the helix 3[10](III) between Asl1650 (blue) and TycC3 PCP (green). The backbone is represented by a spline function through the C^[alpha] positions, and the side chain heavy atoms are shown as stick diagrams. The orientation is such that side chains in the front right of the figure are exposed on the protein surface.

The above figures are reprinted from an Open Access publication published by the Protein Society: Protein Sci (2006, 15, 1030-1041) copyright 2006.

Figures were selected by an automated process.