1NM8

Structure of Human Carnitine Acetyltransferase: Molecular Basis for Fatty Acyl Transfer


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.60 Å
  • R-Value Free: 0.232 
  • R-Value Work: 0.208 

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This is version 1.3 of the entry. See complete history


Literature

Structure of Human Carnitine Acetyltransferase. Molecular Basis for Fatty Acyl Transfer

Wu, D.Govindasamy, L.Lian, W.Gu, Y.Kukar, T.Agbandje-McKenna, M.McKenna, R.

(2003) J Biol Chem 278: 13159-13165

  • DOI: https://doi.org/10.1074/jbc.M212356200
  • Primary Citation of Related Structures:  
    1NM8

  • PubMed Abstract: 

    Carnitine acyltransferases are a family of ubiquitous enzymes that play a pivotal role in cellular energy metabolism. We report here the x-ray structure of human carnitine acetyltransferase to a 1.6-A resolution. This structure reveals a monomeric protein of two equally sized alpha/beta domains. Each domain is shown to have a partially similar fold to other known but oligomeric enzymes that are also involved in group-transfer reactions. The unique monomeric arrangement of the two domains constitutes a central narrow active site tunnel, indicating a likely universal feature for all members of the carnitine acyltransferase family. Superimposition of the substrate complex of a related protein, dihydrolipoyl trans-acetylase, reveals that both substrates localize to the active site tunnel of human carnitine acetyltransferase, suggesting the location of the ligand binding sites for carnitine and coenzyme A. Most significantly, this structure provides critical insights into the molecular basis for fatty acyl chain transfer and a possible common mechanism among a wide range of acyltransferases utilizing a catalytic dyad.


  • Organizational Affiliation

    Department of Medicinal Chemistry, College of Pharmacy, University of Florida, Gainesville, Florida 32610, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Carnitine O-acetyltransferase616Homo sapiensMutation(s): 3 
Gene Names: CRAT OR CAT1
EC: 2.3.1.7
Membrane Entity: Yes 
UniProt & NIH Common Fund Data Resources
Find proteins for P43155 (Homo sapiens)
Explore P43155 
Go to UniProtKB:  P43155
PHAROS:  P43155
GTEx:  ENSG00000095321 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP43155
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.60 Å
  • R-Value Free: 0.232 
  • R-Value Work: 0.208 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 137.5α = 90
b = 84.5β = 90
c = 57.5γ = 90
Software Package:
Software NamePurpose
DENZOdata reduction
SCALEPACKdata scaling
CNSrefinement
CNSphasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2003-03-11
    Type: Initial release
  • Version 1.1: 2008-04-29
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2024-02-14
    Changes: Data collection, Database references