2LIU

NMR structure of holo-ACPI domain from CurA module from Lyngbya majuscula


Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Calculated: 100 
  • Conformers Submitted: 20 
  • Selection Criteria: target function 

wwPDB Validation   3D Report Full Report


This is version 1.4 of the entry. See complete history


Literature

Characterization of Molecular Interactions between ACP and Halogenase Domains in the Curacin A Polyketide Synthase.

Busche, A.Gottstein, D.Hein, C.Ripin, N.Pader, I.Tufar, P.Eisman, E.B.Gu, L.Walsh, C.T.Sherman, D.H.Lohr, F.Guntert, P.Dotsch, V.

(2012) ACS Chem Biol 7: 378-386

  • DOI: https://doi.org/10.1021/cb200352q
  • Primary Citation of Related Structures:  
    2LIU, 2LIW

  • PubMed Abstract: 

    Polyketide synthases (PKSs) and non-ribosomal peptide synthetases (NRPSs) are large multidomain proteins present in microorganisms that produce bioactive compounds. Curacin A is such a bioactive compound with potent anti-proliferative activity. During its biosynthesis the growing substrate is bound covalently to an acyl carrier protein (ACP) that is able to access catalytic sites of neighboring domains for chain elongation and modification. While ACP domains usually occur as monomers, the curacin A cluster codes for a triplet ACP (ACP(I)-ACP(II)-ACP(III)) within the CurA PKS module. We have determined the structure of the isolated holo-ACP(I) and show that the ACPs are independent of each other within this tridomain system. In addition, we have determined the structure of the 3-hydroxyl-3-methylglutaryl-loaded holo-ACP(I), which is the substrate for the unique halogenase (Hal) domain embedded within the CurA module. We have identified the interaction surface of both proteins using mutagenesis and MALDI-based identification of product formation. Amino acids affecting product formation are located on helices II and III of ACP(I) and form a contiguous surface. Since the CurA Hal accepts substrate only when presented by one of the ACPs within the ACP(I)-ACP(II)-ACP(III) tridomain, our data provide insight into the specificity of the chlorination reaction.


  • Organizational Affiliation

    Institute of Biophysical Chemistry, Goethe University Frankfurt and Center for Biomolecular Magnetic Resonance, Frankfurt am Main, Germany.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
CurA99Lyngbya majusculaMutation(s): 0 
Gene Names: curA
UniProt
Find proteins for Q6DNF2 (Lyngbya majuscula)
Explore Q6DNF2 
Go to UniProtKB:  Q6DNF2
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ6DNF2
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Calculated: 100 
  • Conformers Submitted: 20 
  • Selection Criteria: target function 

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2011-12-14
    Type: Initial release
  • Version 1.1: 2011-12-21
    Changes: Structure summary
  • Version 1.2: 2012-03-14
    Changes: Database references
  • Version 1.3: 2023-06-14
    Changes: Data collection, Database references, Other
  • Version 1.4: 2024-05-15
    Changes: Data collection, Database references