PDBsum entry 5e5n

Hydrolase

PDB id: 5e5n

Contents

Protein chains

563 a.a.

533 a.a.

Waters ×1358

PDB id:

5e5n

Name:

Hydrolase

Title:

Ketosynthase from module 6 of the bacillaene synthase from bacillus subtilis 168 (c167s mutant, crystal form 1)

Structure:

Polyketide synthase pksl. Chain: a, b, c, d. Synonym: pks. Engineered: yes. Mutation: yes

Source:

Bacillus subtilis (strain 168). Organism_taxid: 224308. Strain: 168. Gene: pksl, outg, pksa, pksx, bsu17190. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

2.00Å R-factor: 0.204 R-free: 0.236

Authors:

D.T.Wagner,D.C.Gay,A.T.Keatinge-Clay

Key ref:

D.C.Gay et al. (2016). The LINKS motif zippers trans-acyltransferase polyketide synthase assembly lines into a biosynthetic megacomplex. J Struct Biol, 193, 196-205. PubMed id: 26724270 DOI: 10.1016/j.jsb.2015.12.011

Date:

08-Oct-15 Release date: 18-Nov-15

Protein chains

Q05470  (PKSL_BACSU) -  Polyketide synthase PksL from Bacillus subtilis (strain 168)

Seq: 4538 a.a.

Struc: 563 a.a.*

Protein chains

Q05470  (PKSL_BACSU) -  Polyketide synthase PksL from Bacillus subtilis (strain 168)

Seq: 4538 a.a.

Struc: 533 a.a.*

* PDB and UniProt seqs differ at 2 residue positions (black crosses)

DOI no: 10.1016/j.jsb.2015.12.011

J Struct Biol 193:196-205 (2016)

PubMed id: 26724270

The LINKS motif zippers trans-acyltransferase polyketide synthase assembly lines into a biosynthetic megacomplex.

D.C.Gay, D.T.Wagner, J.L.Meinke, C.E.Zogzas, G.R.Gay, A.T.Keatinge-Clay.

ABSTRACT

Polyketides such as the clinically-valuable antibacterial agent mupirocin are constructed by architecturally-sophisticated assembly lines known as trans-acyltransferase polyketide synthases. Organelle-sized megacomplexes composed of several copies of trans-acyltransferase polyketide synthase assembly lines have been observed by others through transmission electron microscopy to be located at the Bacillus subtilis plasma membrane, where the synthesis and export of the antibacterial polyketide bacillaene takes place. In this work we analyze ten crystal structures of trans-acyltransferase polyketide synthases ketosynthase domains, seven of which are reported here for the first time, to characterize a motif capable of zippering assembly lines into a megacomplex. While each of the three-helix LINKS (Laterally-INteracting Ketosynthase Sequence) motifs is observed to similarly dock with a spatially-reversed copy of itself through hydrophobic and ionic interactions, the amino acid sequences of this motif are not conserved. Such a code is appropriate for mediating homotypic contacts between assembly lines to ensure the ordered self-assembly of a noncovalent, yet tightly-knit, enzymatic network. LINKS-mediated lateral interactions would also have the effect of bolstering the vertical association of the polypeptides that comprise a polyketide synthase assembly line.