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6RCX

Mycobacterial 4'-phosphopantetheinyl transferase PptAb in complex with the ACP domain of PpsC.

Summary for 6RCX
Entry DOI10.2210/pdb6rcx/pdb
Related6QWU 6QXQ 6QXR 6QYF 6QYG
DescriptorPossible 4'-phosphopantetheinyl transferase, Phthiocerol synthesis polyketide synthase type I PpsC, COENZYME A, ... (6 entities in total)
Functional Keywordstransferase/transport protein, transferase-transport protein complex
Biological sourceMycobacteroides abscessus ATCC 19977
More
Total number of polymer chains2
Total formula weight43293.05
Authors
Nguyen, M.C.,Mourey, L.,Pedelacq, J.D. (deposition date: 2019-04-12, release date: 2020-04-15, Last modification date: 2024-01-24)
Primary citationNguyen, M.C.,Saurel, O.,Carivenc, C.,Gavalda, S.,Saitta, S.,Tran, M.P.,Milon, A.,Chalut, C.,Guilhot, C.,Mourey, L.,Pedelacq, J.D.
Conformational flexibility of coenzyme A and its impact on the post-translational modification of acyl carrier proteins by 4'-phosphopantetheinyl transferases.
Febs J., 287:4729-4746, 2020
Cited by
PubMed Abstract: One central question surrounding the biosynthesis of fatty acids and polyketide-derived natural products is how the 4'-phosphopantetheinyl transferase (PPTase) interrogates the essential acyl carrier protein (ACP) domain to fulfill the initial activation step. The triggering factor of this study was the lack of structural information on PPTases at physiological pH, which could bias our comprehension of the mechanism of action of these important enzymes. Structural and functional studies on the family II PPTase PptAb of Mycobacterium abscessus show that pH has a profound effect on the coordination of metal ions and on the conformation of endogenously bound coenzyme A (CoA). The observed conformational flexibility of CoA at physiological pH is accompanied by a disordered 4'-phosphopantetheine (Ppant) moiety. Finally, structural and dynamical information on an isolated mycobacterial ACP domain, in its apo form and in complex with the activator PptAb, suggests an alternate mechanism for the post-translational modification of modular megasynthases.
PubMed: 32128972
DOI: 10.1111/febs.15273
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2 Å)
Structure validation

226707

數據於2024-10-30公開中

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