PDBsum entry 2n98

Transport protein

PDB id: 2n98

Contents

Protein chain

90 a.a.

PDB id:

2n98

Name:

Transport protein

Title:

Solution structure of acyl carrier protein lipd from actinoplanes friuliensis

Structure:

Acyl carrier protein. Chain: a. Engineered: yes

Source:

Actinoplanes friuliensis. Organism_taxid: 196914. Gene: lipd. Expressed in: escherichia coli. Expression_system_taxid: 469008.

NMR struc:

30 models

Authors:

S.Paul,H.Ishida,Z.Liu,L.T.Nguyen,H.J.Vogel

Key ref:

S.Paul et al. (2017). Structural and dynamic characterization of a freestanding acyl carrier protein involved in the biosynthesis of cyclic lipopeptide antibiotics. Protein Sci, 26, 946-959. PubMed id: 28187530

Date:

10-Nov-15 Release date: 16-Nov-16

Protein chain

Q4H1C9  (Q4H1C9_9ACTN) -  Acyl carrier protein from Actinoplanes friuliensis

Seq: 88 a.a.

Struc: 90 a.a.

Enzyme reactions

• Enzyme class: E.C.?

Protein Sci 26:946-959 (2017)

PubMed id: 28187530

Structural and dynamic characterization of a freestanding acyl carrier protein involved in the biosynthesis of cyclic lipopeptide antibiotics.

S.Paul, H.Ishida, L.T.Nguyen, Z.Liu, H.J.Vogel.

ABSTRACT

Friulimicin is a cyclic lipodecapeptide antibiotic that is produced by Actinoplanes friuliensis. Similar to the related lipopeptide drug daptomycin, the peptide skeleton of friulimicin is synthesized by a large multienzyme nonribosomal peptide synthetase (NRPS) system. The LipD protein plays a major role in the acylation reaction of friulimicin. The attachment of the fatty acid group promotes its antibiotic activity. Phylogenetic analysis reveals that LipD is most closely related to other freestanding acyl carrier proteins (ACPs), for which the genes are located near to NRPS gene clusters. Here, we report that the solution NMR structure of apo-LipD is very similar to other four-helix bundle forming ACPs from fatty acid synthase (FAS), polyketide synthase, and NRPS systems. By recording NMR dynamics data, we found that the backbone motions in holo-LipD are more restricted than in apo-LipD due to the attachment of phosphopantetheine moiety. This enhanced stability of holo-LipD was also observed in differential scanning calorimetry experiments. Furthermore, we demonstrate that, unlike several other ACPs, the folding of LipD does not depend on the presence of divalent cations, although the presence of Mg(2+) or Ca(2+) can increase the protein stability. We propose that small structural rearrangements in the tertiary structure of holo-LipD which lead to the enhanced stability are important for the cognate enzyme recognition for the acylation reaction. Our results also highlight the different surface charges of LipD and FAS-ACP from A. friuliensis that would allow the acyl-CoA ligase to interact preferentially with the LipD instead of binding to the FAS-ACP.