1NX8

Structure of carbapenem synthase (CarC) complexed with N-acetyl proline


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.30 Å
  • R-Value Free: 0.275 
  • R-Value Work: 0.228 
  • R-Value Observed: 0.230 

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Ligand Structure Quality Assessment 


This is version 2.0 of the entry. See complete history


Literature

Crystal structure of carbapenem synthase (CarC).

Clifton, I.J.Doan, L.X.Sleeman, M.C.Topf, M.Suzuki, H.Wilmouth, R.C.Schofield, C.J.

(2003) J Biol Chem 278: 20843-20850

  • DOI: https://doi.org/10.1074/jbc.M213054200
  • Primary Citation of Related Structures:  
    1NX4, 1NX8

  • PubMed Abstract: 

    The proposed biosynthetic pathway to the carbapenem antibiotics proceeds via epimerization/desaturation of a carbapenam in an unusual process catalyzed by an iron- and 2-oxoglutarate-dependent oxygenase, CarC. Crystal structures of CarC complexed with Fe(II) and 2-oxoglutarate reveal it to be hexameric (space group C2221), consistent with solution studies. CarC monomers contain a double-stranded beta-helix core that supports ligands binding a single Fe(II) to which 2-oxoglutarate complexes in a bi-dentate manner. A structure was obtained with l-N-acetylproline acting as a substrate analogue. Quantum mechanical/molecular mechanical modeling studies with stereoisomers of carbapenams and carbapenems were used to investigate substrate binding. The combined work will stimulate further mechanistic studies and aid in the engineering of carbapenem biosynthesis.


  • Organizational Affiliation

    Oxford Centre for Molecular Sciences and The Dyson Perrins Laboratory, South Parks Road, Oxford OX1 3QZ, United Kingdom.


Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Carbapenem synthase
A, B, C
273Pectobacterium carotovorumMutation(s): 0 
Gene Names: CarC
UniProt
Find proteins for Q9XB59 (Pectobacterium carotovorum subsp. carotovorum)
Explore Q9XB59 
Go to UniProtKB:  Q9XB59
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ9XB59
Sequence Annotations
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  • Reference Sequence
Small Molecules
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.30 Å
  • R-Value Free: 0.275 
  • R-Value Work: 0.228 
  • R-Value Observed: 0.230 
  • Space Group: C 2 2 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 80.443α = 90
b = 164.082β = 90
c = 146.33γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
MOSFLMdata reduction
CCP4data scaling
AMoREphasing

Structure Validation

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Ligand Structure Quality Assessment 


Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2003-06-17
    Type: Initial release
  • Version 1.1: 2008-04-29
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Advisory, Version format compliance
  • Version 1.3: 2012-07-11
    Changes: Non-polymer description
  • Version 1.4: 2016-08-17
    Changes: Non-polymer description
  • Version 2.0: 2023-08-16
    Changes: Advisory, Atomic model, Data collection, Database references, Derived calculations, Refinement description