7uk4

KS-AT di-domain of mycobacterial Pks13 with endogenous KS ligand bound

spinqualitylabelsall models 7uk4, resolution 1.94Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7uk4 is a 2 chain structure with sequence from Mycolicibacterium smegmatis MC2 155. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 1.94Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function I7FMV0_MYCS2 Publication Abstract from PubMed 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 A 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. Structure and dynamics of the essential endogenous mycobacterial polyketide synthase Pks13.,Kim SK, Dickinson MS, Finer-Moore J, Guan Z, Kaake RM, Echeverria I, Chen J, Pulido EH, Sali A, Krogan NJ, Rosenberg OS, Stroud RM Nat Struct Mol Biol. 2023 Mar;30(3):296-308. doi: 10.1038/s41594-022-00918-0. , Epub 2023 Feb 13. PMID:36782050 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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