2RCU

Crystal structure of rat carnitine palmitoyltransferase 2 in complex with r-3-(hexadecanoylamino)-4-(trimethylazaniumyl)butanoate

Summary for 2RCU

• Entry DOI: 10.2210/pdb2rcu/pdb
• Related: 2deb 2fw3 2fyo 2h4t
• Descriptor: Carnitine O-palmitoyltransferase 2, octyl beta-D-glucopyranoside, (3R)-3-(hexadecanoylamino)-4-(trimethylammonio)butanoate, ... (4 entities in total)
• Functional Keywords: transferase, acyltransferase, mitochondrial protein, acetylation, fatty acid metabolism, inner membrane, lipid metabolism, membrane, mitochondrion, transit peptide, transport, transferase 04-mai-06 r
• Biological source: Rattus norvegicus (Norway rat)
• Total number of polymer chains: 2
• Total formula weight: 148221.80

Authors

Rufer, A.C.,Benz, J.,Chomienne, O.,Thoma, R.,Hennig, M. (deposition date: 2007-09-20, release date: 2007-10-16, Last modification date: 2023-08-30)

Primary citation

Rufer, A.C.,Lomize, A.,Benz, J.,Chomienne, O.,Thoma, R.,Hennig, M.
Carnitine palmitoyltransferase 2: analysis of membrane association and complex structure with a substrate analog.
Febs Lett., 581:3247-3252, 2007

PubMed Abstract: The mitochondrial membrane-associated carnitine palmitoyltransferase system is a validated target for the treatment of type 2 diabetes mellitus. To further facilitate structure-based drug discovery, we determined the crystal structure of rat CPT-2 (rCPT-2) in complex with the substrate analogue palmitoyl-aminocarnitine at 1.8A resolution. Biochemical analyses revealed a strong effect of this compound on rCPT-2 activity and stability. Using a computational approach we examined the membrane association of rCPT-2. The protein interacts with the membrane as a functional monomer and the calculations confirm the presence of a membrane association domain that consists of layers of hydrophobic and positively charged residues.

PubMed: 17585909
DOI: 10.1016/j.febslet.2007.05.080

Experimental method

X-RAY DIFFRACTION (1.78 Å)