2WDS

Crystal structure of the Streptomyces coelicolor H110A AcpS mutant in complex with cofactor CoA at 1.3 A


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.35 Å
  • R-Value Free: 0.205 
  • R-Value Work: 0.183 
  • R-Value Observed: 0.184 

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Ligand Structure Quality Assessment 


This is version 1.2 of the entry. See complete history


Literature

Analysis of Streptomyces Coelicolor Phosphopantetheinyl Transferase, Acps, Reveals the Basis for Relaxed Substrate Specificity.

Dall'Aglio, P.Arthur, C.Williams, C.Vasilakis, K.Maple, H.J.Crosby, J.Crump, M.P.Hadfield, A.T.

(2011) Biochemistry 50: 5704

  • DOI: https://doi.org/10.1021/bi2003668
  • Primary Citation of Related Structures:  
    2JBZ, 2JCA, 2WDO, 2WDS, 2WDY

  • PubMed Abstract: 

    The transfer of the phosphopantetheine chain from coenzyme A (CoA) to the acyl carrier protein (ACP), a key protein in both fatty acid and polyketide synthesis, is catalyzed by ACP synthase (AcpS). Streptomyces coelicolor AcpS is a doubly promiscuous enzyme capable of activation of ACPs from both fatty acid and polyketide synthesis and catalyzes the transfer of modified CoA substrates. Five crystal structures have been determined, including those of ligand-free AcpS, complexes with CoA and acetyl-CoA, and two of the active site mutants, His110Ala and Asp111Ala. All five structures are trimeric and provide further insight into the mechanism of catalysis, revealing the first detailed structure of a group I active site with the essential magnesium in place. Modeling of ACP binding supported by mutational analysis suggests an explanation for the promiscuity in terms of both ACP partner and modified CoA substrates.


  • Organizational Affiliation

    Department of Biochemistry, School of Medical Sciences, University of Bristol, University Walk, Clifton, Bristol BS8 1TD, U.K.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
HOLO-[ACYL-CARRIER-PROTEIN] SYNTHASE143Streptomyces coelicolorMutation(s): 1 
EC: 2.7.8.7
UniProt
Find proteins for O86785 (Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145))
Explore O86785 
Go to UniProtKB:  O86785
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupO86785
Sequence Annotations
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  • Reference Sequence
Small Molecules
Binding Affinity Annotations 
IDSourceBinding Affinity
COA Binding MOAD:  2WDS Kd: 450 (nM) from 1 assay(s)
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.35 Å
  • R-Value Free: 0.205 
  • R-Value Work: 0.183 
  • R-Value Observed: 0.184 
  • Space Group: P 21 3
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 72.719α = 90
b = 72.719β = 90
c = 72.719γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
DENZOdata reduction
SCALEPACKdata scaling
PHASERphasing

Structure Validation

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Ligand Structure Quality Assessment 


Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2010-04-21
    Type: Initial release
  • Version 1.1: 2011-11-16
    Changes: Database references, Derived calculations, Non-polymer description, Other, Version format compliance
  • Version 1.2: 2023-12-13
    Changes: Data collection, Database references, Derived calculations, Other, Refinement description