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Structure paper

TitleStructure and dynamics of the essential endogenous mycobacterial polyketide synthase Pks13.
Journal, issue, pagesNat Struct Mol Biol, Vol. 30, Issue 3, Page 296-308, Year 2023
Publish dateFeb 13, 2023
AuthorsSun Kyung Kim / Miles Sasha Dickinson / Janet Finer-Moore / Ziqiang Guan / Robyn M Kaake / Ignacia Echeverria / Jen Chen / Ernst H Pulido / Andrej Sali / Nevan J Krogan / Oren S Rosenberg / Robert M Stroud /
PubMed AbstractThe mycolic acid layer of the Mycobacterium tuberculosis cell wall is essential for viability and virulence, and the enzymes responsible for its synthesis are targets for antimycobacterial drug ...The mycolic acid layer of the Mycobacterium tuberculosis cell wall is essential for viability and virulence, and the enzymes responsible for its synthesis are targets for antimycobacterial drug development. Polyketide synthase 13 (Pks13) is a module encoding several enzymatic and transport functions that carries out the condensation of two different long-chain fatty acids to produce mycolic acids. We determined structures by cryogenic-electron microscopy of dimeric multi-enzyme Pks13 purified from mycobacteria under normal growth conditions, captured with native substrates. Structures define the ketosynthase (KS), linker and acyl transferase (AT) domains at 1.8 Å resolution and two alternative locations of the N-terminal acyl carrier protein. These structures suggest intermediate states on the pathway for substrate delivery to the KS domain. Other domains, visible at lower resolution, are flexible relative to the KS-AT core. The chemical structures of three bound endogenous long-chain fatty acid substrates were determined by electrospray ionization mass spectrometry.
External linksNat Struct Mol Biol / PubMed:36782050 / PubMed Central
MethodsEM (single particle)
Resolution1.94 - 3.1 Å
Structure data

26574

7uk4

EMDB-26574, PDB-7uk4:
KS-AT di-domain of mycobacterial Pks13 with endogenous KS ligand bound
Method: EM (single particle) / Resolution: 1.94 Å

27002

8cuy

EMDB-27002, PDB-8cuy:
ACP1-KS-AT domains of mycobacterial Pks13
Method: EM (single particle) / Resolution: 2.4 Å

27003

8cuz

EMDB-27003, PDB-8cuz:
KS-AT domains of mycobacterial Pks13 with inward AT conformation
Method: EM (single particle) / Resolution: 3.0 Å

27004

8cv0

EMDB-27004, PDB-8cv0:
KS-AT domains of mycobacterial Pks13 with outward AT conformation
Method: EM (single particle) / Resolution: 3.1 Å

27005

8cv1

EMDB-27005, PDB-8cv1:
ACP1-KS-AT domains of mycobacterial Pks13
Method: EM (single particle) / Resolution: 2.6 Å

Chemicals


ChemComp, No image

ChemComp-UNL:
Unknown ligand

ChemComp-HOH:
WATER / Water

ChemComp-PNS:
4'-PHOSPHOPANTETHEINE / Phosphopantetheine

Source
  • mycolicibacterium smegmatis mc2 155 (bacteria)
KeywordsBIOSYNTHETIC PROTEIN / mycolic acid synthesis / ketosynthase / acyltransferase / multi-domain assembly / acyl carrier protein

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