3R44

Mycobacterium tuberculosis fatty acyl CoA synthetase

Summary for 3R44

• Entry DOI: 10.2210/pdb3r44/pdb
• Descriptor: fatty acyl CoA synthetase FADD13 (FATTY-ACYL-CoA SYNTHETASE), HISTIDINE, MALONATE ION, ... (4 entities in total)
• Functional Keywords: acyl coa synthetase, ligase
• Biological source: Mycobacterium tuberculosis
• Total number of polymer chains: 1
• Total formula weight: 56492.25

Authors

Andersson, C.S.,Martinez Molina, D.,Hogbom, M. (deposition date: 2011-03-17, release date: 2012-02-08, Last modification date: 2023-09-13)

Primary citation

Andersson, C.S.,Lundgren, C.A.,Magnusdottir, A.,Ge, C.,Wieslander, A.,Martinez Molina, D.,Hogbom, M.
The Mycobacterium tuberculosis Very-Long-Chain Fatty Acyl-CoA Synthetase: Structural Basis for Housing Lipid Substrates Longer than the Enzyme.
Structure, 20:1062-1070, 2012

PubMed Abstract: The Mycobacterium tuberculosis acid-induced operon MymA encodes the fatty acyl-CoA synthetase FadD13 and is essential for virulence and intracellular growth of the pathogen. Fatty acyl-CoA synthetases activate lipids before entering into the metabolic pathways and are also involved in transmembrane lipid transport. Unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length tested (C(26)). Here, we show that FadD13 is a peripheral membrane protein. The structure and mutational studies reveal an arginine- and aromatic-rich surface patch as the site for membrane interaction. The protein accommodates a hydrophobic tunnel that extends from the active site toward the positive patch and is sealed by an arginine-rich lid-loop at the protein surface. Based on this and previous data, we propose a structural basis for accommodation of lipid substrates longer than the enzyme and transmembrane lipid transport by vectorial CoA-esterification.

PubMed: 22560731
DOI: 10.1016/j.str.2012.03.012

Experimental method

X-RAY DIFFRACTION (1.8 Å)