6JOM

Crystal structure of lipoate protein ligase from Mycoplasma hyopneumoniae

Summary for 6JOM

• Entry DOI: 10.2210/pdb6jom/pdb
• Descriptor: Lipoate--protein ligase, 5'-O-[(R)-({5-[(3R)-1,2-DITHIOLAN-3-YL]PENTANOYL}OXY)(HYDROXY)PHOSPHORYL]ADENOSINE (3 entities in total)
• Functional Keywords: mycoplasma hyopneumoniae, lipoate protein ligase, lpl, lipoyl-amp, ligase
• Biological source: Mycoplasma hyopneumoniae J
• Total number of polymer chains: 2
• Total formula weight: 82746.85

Authors

Zhang, H.,Chen, H.,Ma, G. (deposition date: 2019-03-22, release date: 2020-03-25, Last modification date: 2024-03-27)

Primary citation

Zhu, K.,Chen, H.,Jin, J.,Wang, N.,Ma, G.,Huang, J.,Feng, Y.,Xin, J.,Zhang, H.,Liu, H.
Functional Identification and Structural Analysis of a New Lipoate Protein Ligase inMycoplasma hyopneumoniae.
Front Cell Infect Microbiol, 10:156-156, 2020

PubMed Abstract: () is the causative agent of pandemic pneumonia among pigs, namely, swine enzootic pneumonia. Although was first identified in 1965, little is known regarding its metabolic pathways, which might play a pivotal role during disease pathogenesis. Lipoate is an essential cofactor for enzymes important for central metabolism. However, the lipoate metabolism pathway in is definitely unclear. Here, we identified a novel gene, lpl, encoding a lipoate protein ligase in the genome of (Mhp-Lpl). This gene contains 1,032 base pairs and encodes a protein of 343 amino acids, which is between 7.5 and 36.09% identical to lipoate protein ligases (Lpls) of other species. Similar to its homologs in other species, Mhp-Lpl catalyzes the ATP-dependent activation of lipoate to lipoyl-AMP and the transfer of the activated lipoyl onto the lipoyl domains of GcvH (Mhp H) . Enzymatic and mutagenesis analysis indicate that residue K56 within the SKT sequence of Mhp H protein is the lipoyl moiety acceptor site. The three-dimensional structure showed typical lipoate protein ligase folding, with a large N-terminal domain and a small C-terminal domain. The large N-terminal domain is responsible for the full enzymatic activity of Mhp-Lpl. The identification and characterization of Mhp-Lpl will be beneficial to our understanding of metabolism.

PubMed: 32373550
DOI: 10.3389/fcimb.2020.00156

Experimental method

X-RAY DIFFRACTION (2.45 Å)