Protein Family Models

This entry represents the catalytic domain of a group of lipoyl ligases/lipoyltransferases, such as Lipoate-protein ligase A/B (LipA/B) from E.coli and mammalian lipoyltransferases [1-5]. These proteins catalyse the transfer of the lipoyl group from lipoyl-AMP to the specific lysine residue of lipoyl domains of lipoate-dependent enzymes. Lipoic acid is an essential cofactor of the alpha-ketoacid dehydrogenase complexes and the glycine cleavage system. Paper describing PDB structure 1w66. [1]. 16735476. The Mycobacterium tuberculosis LipB enzyme functions as a cysteine/lysine dyad acyltransferase. Ma Q, Zhao X, Nasser Eddine A, Geerlof A, Li X, Cronan JE, Kaufmann SH, Wilmanns M;. Proc Natl Acad Sci U S A. 2006;103:8662-8667. Paper describing PDB structure 1x2g. [2]. 16043486. Crystal structure of lipoate-protein ligase A from Escherichia coli. Determination of the lipoic acid-binding site. Fujiwara K, Toma S, Okamura-Ikeda K, Motokawa Y, Nakagawa A, Taniguchi H;. J Biol Chem. 2005;280:33645-33651. Paper describing PDB structure 2ars. [3]. 16141198. Crystal structure of lipoate-protein ligase A bound with the activated intermediate: insights into interaction with lipoyl domains. Kim DJ, Kim KH, Lee HH, Lee SJ, Ha JY, Yoon HJ, Suh SW;. J Biol Chem. 2005;280:38081-38089. Paper describing PDB structure 2c7i. [4]. 16384580. Structure of a putative lipoate protein ligase from Thermoplasma acidophilum and the mechanism of target selection for post-translational modification. McManus E, Luisi BF, Perham RN;. J Mol Biol. 2006;356:625-637. Paper describing PDB structure 2e5a. [5]. 17570395. Crystal structure of bovine lipoyltransfer. TRUNCATED at 1650 bytes (from Pfam)

Date:

2024-10-21

lipoate--protein ligase (LPL) family protein is responsible for attaching lipoic acid to a specific lysine at the active site of lipoate-dependent enzymes

Date:

2017-06-28