PDBsum entry 6tdd

Protein binding

PDB id: 6tdd

Contents

Protein chains

45 a.a.

PDB id:

6tdd

Name:

Protein binding

Title:

Bam_5924 docking domain

Structure:

Beta-ketoacyl synthase. Chain: a, b. Engineered: yes. Other_details: dimeric protein

Source:

Burkholderia ambifaria ammd. Organism_taxid: 339670. Gene: bamb_5924. Expressed in: escherichia coli. Expression_system_taxid: 562.

NMR struc:

25 models

Authors:

F.Risser,B.Chagot

Key ref:

F.Risser et al. (2020). Towards improved understanding of intersubunit interactions in modular polyketide biosynthesis: Docking in the enacyloxin IIa polyketide synthase. J Struct Biol, 212, 107581. PubMed id: 32717326 DOI: 10.1016/j.jsb.2020.107581

Date:

08-Nov-19 Release date: 12-Aug-20

Protein chains

Q0B304  (Q0B304_BURCM) -  Beta-ketoacyl synthase from Burkholderia ambifaria (strain ATCC BAA-244 / DSM 16087 / CCUG 44356 / LMG 19182 / AMMD)

Seq: 2201 a.a.

Struc: 45 a.a.

DOI no: 10.1016/j.jsb.2020.107581

J Struct Biol 212:107581 (2020)

PubMed id: 32717326

Towards improved understanding of intersubunit interactions in modular polyketide biosynthesis: Docking in the enacyloxin IIa polyketide synthase.

F.Risser, S.Collin, R.Dos Santos-Morais, A.Gruez, B.Chagot, K.J.Weissman.

ABSTRACT

Modular polyketide synthases (PKSs) are molecular-scale assembly lines comprising multiple gigantic polypeptide subunits. Faithful ordering of the subunits is mediated by extreme C- and N-terminal regions called docking domains (DDs). Decrypting how specificity is achieved by these elements is important both for understanding PKS function and modifying it to generate useful polyketide analogues for biological evaluation. Here we report the biophysical and structural characterisation of all six PKS/PKS interfaces in the unusual, chimaeric cis-AT/trans-AT PKS pathway responsible for biosynthesis of the antibiotic enacyloxin IIa in Burkholderia ambifaria. Taken together with previous work, our data reveal that specificity is achieved in the enacyloxin PKS by deploying at least three functionally orthogonal classes of DDs. We also demonstrate for the first time that cis-AT PKS subunits incorporate DDs with intrinsically disordered character, reinforcing the utility of such regions for achieving both medium affinity and high specificity at PKS intersubunit junctions. Overall, this work substantially increases the number of orthogonal DDs available for creating novel, highly-specific interfaces within cis- and trans-AT PKSs and their hybrids. It also reveals unexpected sequence/structure relationships in PKS DDs, identifying major current limitations to both accurately predicting and categorising these useful protein-protein interaction motifs.