6RCX

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


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.00 Å
  • R-Value Free: 0.244 
  • R-Value Work: 0.206 
  • R-Value Observed: 0.208 

wwPDB Validation   3D Report Full Report


Ligand Structure Quality Assessment 


This is version 1.2 of the entry. See complete history


Literature

Conformational flexibility of coenzyme A and its impact on the post-translational modification of acyl carrier proteins by 4'-phosphopantetheinyl transferases.

Nguyen, M.C.Saurel, O.Carivenc, C.Gavalda, S.Saitta, S.Tran, M.P.Milon, A.Chalut, C.Guilhot, C.Mourey, L.Pedelacq, J.D.

(2020) FEBS J 287: 4729-4746

  • DOI: https://doi.org/10.1111/febs.15273
  • Primary Citation of Related Structures:  
    6QWU, 6QXQ, 6QXR, 6QYF, 6QYG, 6RCX

  • 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.


  • Organizational Affiliation

    Institut de Pharmacologie et de Biologie Structurale (IPBS), Université de Toulouse, CNRS, UPS, Toulouse, France.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Possible 4'-phosphopantetheinyl transferase232Mycobacteroides abscessus ATCC 19977Mutation(s): 0 
Gene Names: MAB_3117c
UniProt
Find proteins for B1MD73 (Mycobacteroides abscessus (strain ATCC 19977 / DSM 44196 / CCUG 20993 / CIP 104536 / JCM 13569 / NCTC 13031 / TMC 1543 / L948))
Explore B1MD73 
Go to UniProtKB:  B1MD73
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupB1MD73
Sequence Annotations
Expand
  • Reference Sequence
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
Phthiocerol synthesis polyketide synthase type I PpsC157Mycobacteroides abscessus ATCC 19977Mutation(s): 1 
Gene Names: ppsCRv2933
EC: 2.3.1.41
UniProt
Find proteins for P96202 (Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv))
Explore P96202 
Go to UniProtKB:  P96202
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP96202
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.00 Å
  • R-Value Free: 0.244 
  • R-Value Work: 0.206 
  • R-Value Observed: 0.208 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 50.142α = 90
b = 63.167β = 90
c = 108.459γ = 90
Software Package:
Software NamePurpose
PHENIXrefinement
PHASERphasing
TRUNCATEdata reduction
XDSdata scaling

Structure Validation

View Full Validation Report



Ligand Structure Quality Assessment 


Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
European Union (EU)France10559
French National Research AgencyFranceANR-16-CE18-0011-01

Revision History  (Full details and data files)

  • Version 1.0: 2020-04-15
    Type: Initial release
  • Version 1.1: 2020-11-11
    Changes: Database references, Derived calculations
  • Version 1.2: 2024-01-24
    Changes: Data collection, Database references, Refinement description