2H4T

Crystal structure of rat carnitine palmitoyltransferase II

Summary for 2H4T

• Entry DOI: 10.2210/pdb2h4t/pdb
• Descriptor: Carnitine O-palmitoyltransferase II, mitochondrial, DODECANE (3 entities in total)
• Functional Keywords: carnitine acyltransferase, transferase
• Biological source: Rattus norvegicus (Norway rat)
• Cellular location: Mitochondrion inner membrane ; Peripheral membrane protein ; Matrix side : P18886
• Total number of polymer chains: 2
• Total formula weight: 142467.82

Authors

Hsiao, Y.S.,Jogl, G.,Esser, V.,Tong, L. (deposition date: 2006-05-25, release date: 2006-07-25, Last modification date: 2024-02-14)

Primary citation

Hsiao, Y.S.,Jogl, G.,Esser, V.,Tong, L.
Crystal structure of rat carnitine palmitoyltransferase II (CPT-II).
Biochem.Biophys.Res.Commun., 346:974-980, 2006

PubMed Abstract: Carnitine palmitoyltransferase II (CPT-II) has a crucial role in the beta-oxidation of long-chain fatty acids in mitochondria. We report here the crystal structure of rat CPT-II at 1.9A resolution. The overall structure shares strong similarity to those of short- and medium-chain carnitine acyltransferases, although detailed structural differences in the active site region have a significant impact on the substrate selectivity of CPT-II. Three aliphatic chains, possibly from a detergent that is used for the crystallization, were found in the structure. Two of them are located in the carnitine and CoA binding sites, respectively. The third aliphatic chain may mimic the long-chain acyl group in the substrate of CPT-II. The binding site for this aliphatic chain does not exist in the short- and medium-chain carnitine acyltransferases, due to conformational differences among the enzymes. A unique insert in CPT-II is positioned on the surface of the enzyme, with a highly hydrophobic surface. It is likely that this surface patch mediates the association of CPT-II with the inner membrane of the mitochondria.

PubMed: 16781677
DOI: 10.1016/j.bbrc.2006.06.006

Experimental method

X-RAY DIFFRACTION (1.9 Å)