1NDI

Carnitine Acetyltransferase in complex with CoA

Summary for 1NDI

• Entry DOI: 10.2210/pdb1ndi/pdb
• Related: 1NDB 1NDF
• Descriptor: Carnitine Acetyltransferase, COENZYME A (3 entities in total)
• Functional Keywords: acetyl transfer, coa, coenzyme a, transferase
• Biological source: Mus musculus (house mouse)
• Cellular location: Endoplasmic reticulum (Potential): P47934
• Total number of polymer chains: 2
• Total formula weight: 136897.99

Authors

Jogl, G.,Tong, L. (deposition date: 2002-12-09, release date: 2003-01-28, Last modification date: 2023-08-16)

Primary citation

Jogl, G.,Tong, L.
Crystal Structure of Carnitine Acetyltransferase and Implications for the Catalytic Mechanism and Fatty Acid Transport
Cell(Cambridge,Mass.), 112:113-122, 2003

PubMed Abstract: Carnitine acyltransferases have crucial roles in the transport of fatty acids for beta-oxidation. Dysregulation of these enzymes can lead to serious diseases in humans, and they are targets for therapeutic development against diabetes. We report the crystal structures of murine carnitine acetyltransferase (CRAT), alone and in complex with its substrate carnitine or CoA. The structure contains two domains. Surprisingly, these two domains share the same backbone fold, which is also similar to that of chloramphenicol acetyltransferase and dihydrolipoyl transacetylase. The active site is located at the interface between the two domains. Carnitine and CoA are bound in deep channels in the enzyme, on opposite sides of the catalytic His343 residue. The structural information provides a molecular basis for understanding the catalysis by carnitine acyltransferases and for designing their inhibitors. Specifically, our structural information suggests that the substrate carnitine may assist the catalysis by stabilizing the oxyanion in the reaction intermediate.

PubMed: 12526798
DOI: 10.1016/S0092-8674(02)01228-X

Experimental method

X-RAY DIFFRACTION (2.3 Å)