Functional Identification and Structural Analysis of a New Lipoate Protein Ligase in

Overview

Journal Front Cell Infect Microbiol

Specialties Cell Biology
Infectious Diseases
Microbiology

Date 2020 May 7

PMID 32373550

Citations 5

Authors

Kemeng Zhu

Huan Chen

Jin Jin

Ning Wang

Guixing Ma

Jiandong Huang

Youjun Feng

Jiuqing Xin

Hongmin Zhang

Henggui Liu

Affiliations

Soon will be listed here.

Abstract

Summary: Lipoic acid is an essential cofactor for the activation of some enzyme complexes involved in key metabolic processes. Lipoate protein ligases (Lpls) are responsible for the metabolism of lipoic acid. To date, little is known regarding the Lpls in . In this study, we identified a lipoate protein ligase of . We further analyzed the function, overall structure and ligand-binding site of this protein. The lipoate acceptor site on GcvH was also identified. Together, these findings reveal that Lpl exists in and will provide a basis for further exploration of the pathway of lipoic acid metabolism in .

Citing Articles

Lipoic acid attachment to proteins: stimulating new developments.

Cronan J Microbiol Mol Biol Rev. 2024; 88(2):e0000524.

PMID: 38624243 PMC: 11332335. DOI: 10.1128/mmbr.00005-24.

Identification of a novel lipoic acid biosynthesis pathway reveals the complex evolution of lipoate assembly in prokaryotes.

Tanabe T, Grosser M, Hahn L, Kumpel C, Hartenfels H, Vtulkin E PLoS Biol. 2023; 21(6):e3002177.

PMID: 37368881 PMC: 10332631. DOI: 10.1371/journal.pbio.3002177.

Understanding and Engineering Glycine Cleavage System and Related Metabolic Pathways for C1-Based Biosynthesis.

Ren J, Wang W, Nie J, Yuan W, Zeng A Adv Biochem Eng Biotechnol. 2022; 180:273-298.

PMID: 35294558 DOI: 10.1007/10_2021_186.

Infection strategies of mycoplasmas: Unraveling the panoply of virulence factors.

Yiwen C, Yueyue W, Lianmei Q, Cuiming Z, Xiaoxing Y Virulence. 2021; 12(1):788-817.

PMID: 33704021 PMC: 7954426. DOI: 10.1080/21505594.2021.1889813.

A Novel Lipoate-Protein Ligase, Mhp-LplJ, Is Required for Lipoic Acid Metabolism in .

Jin J, Chen H, Wang N, Zhu K, Liu H, Shi D Front Microbiol. 2021; 11:631433.

PMID: 33584596 PMC: 7873978. DOI: 10.3389/fmicb.2020.631433.

References

. The CCP4 suite: programs for protein crystallography. Acta Crystallogr D Biol Crystallogr. 1994; 50(Pt 5):760-3. DOI: 10.1107/S0907444994003112. View

Pompidor G, Maury O, Vicat J, Kahn R . A dipicolinate lanthanide complex for solving protein structures using anomalous diffraction. Acta Crystallogr D Biol Crystallogr. 2010; 66(Pt 7):762-9. DOI: 10.1107/S0907444910010954. View

Reed L, Hackert M . Structure-function relationships in dihydrolipoamide acyltransferases. J Biol Chem. 1990; 265(16):8971-4. View

Smith A, Shenvi S, Widlansky M, Suh J, Hagen T . Lipoic acid as a potential therapy for chronic diseases associated with oxidative stress. Curr Med Chem. 2004; 11(9):1135-46. DOI: 10.2174/0929867043365387. View

Cronan J, Zhao X, Jiang Y . Function, attachment and synthesis of lipoic acid in Escherichia coli. Adv Microb Physiol. 2005; 50:103-46. DOI: 10.1016/S0065-2911(05)50003-1. View

Reche P, Perham R . Structure and selectivity in post-translational modification: attaching the biotinyl-lysine and lipoyl-lysine swinging arms in multifunctional enzymes. EMBO J. 1999; 18(10):2673-82. PMC: 1171349. DOI: 10.1093/emboj/18.10.2673. View

Terwilliger T . SOLVE and RESOLVE: automated structure solution and density modification. Methods Enzymol. 2003; 374:22-37. DOI: 10.1016/S0076-6879(03)74002-6. View

Cao X, Cronan J . The Streptomyces coelicolor lipoate-protein ligase is a circularly permuted version of the Escherichia coli enzyme composed of discrete interacting domains. J Biol Chem. 2015; 290(11):7280-90. PMC: 4358146. DOI: 10.1074/jbc.M114.626879. View

Christensen Q, Hagar J, ORiordan M, Cronan J . A complex lipoate utilization pathway in Listeria monocytogenes. J Biol Chem. 2011; 286(36):31447-56. PMC: 3173067. DOI: 10.1074/jbc.M111.273607. View

10.

Martin N, Christensen Q, Mansilla M, Cronan J, de Mendoza D . A novel two-gene requirement for the octanoyltransfer reaction of Bacillus subtilis lipoic acid biosynthesis. Mol Microbiol. 2011; 80(2):335-49. PMC: 3086205. DOI: 10.1111/j.1365-2958.2011.07597.x. View

11.

McManus E, Luisi B, Perham R . Structure of a putative lipoate protein ligase from Thermoplasma acidophilum and the mechanism of target selection for post-translational modification. J Mol Biol. 2005; 356(3):625-37. PMC: 7610907. DOI: 10.1016/j.jmb.2005.11.057. View

12.

Maes D, Segales J, Meyns T, Sibila M, Pieters M, Haesebrouck F . Control of Mycoplasma hyopneumoniae infections in pigs. Vet Microbiol. 2007; 126(4):297-309. PMC: 7130725. DOI: 10.1016/j.vetmic.2007.09.008. View

13.

Murshudov G, Skubak P, Lebedev A, Pannu N, Steiner R, Nicholls R . REFMAC5 for the refinement of macromolecular crystal structures. Acta Crystallogr D Biol Crystallogr. 2011; 67(Pt 4):355-67. PMC: 3069751. DOI: 10.1107/S0907444911001314. View

14.

Morris R, Perrakis A, Lamzin V . ARP/wARP and automatic interpretation of protein electron density maps. Methods Enzymol. 2003; 374:229-44. DOI: 10.1016/S0076-6879(03)74011-7. View

15.

Cao X, Hong Y, Zhu L, Hu Y, Cronan J . Development and retention of a primordial moonlighting pathway of protein modification in the absence of selection presents a puzzle. Proc Natl Acad Sci U S A. 2018; 115(4):647-655. PMC: 5789953. DOI: 10.1073/pnas.1718653115. View

16.

Fujiwara K, MOTOKAWA Y . Cloning and expression of a cDNA encoding bovine lipoyltransferase. J Biol Chem. 1998; 272(51):31974-8. DOI: 10.1074/jbc.272.51.31974. View

17.

Sheldrick G . Experimental phasing with SHELXC/D/E: combining chain tracing with density modification. Acta Crystallogr D Biol Crystallogr. 2010; 66(Pt 4):479-85. PMC: 2852312. DOI: 10.1107/S0907444909038360. View

18.

Duckworth B, Geders T, Tiwari D, Boshoff H, Sibbald P, Barry 3rd C . Bisubstrate adenylation inhibitors of biotin protein ligase from Mycobacterium tuberculosis. Chem Biol. 2011; 18(11):1432-41. PMC: 3225891. DOI: 10.1016/j.chembiol.2011.08.013. View

19.

Fujiwara K, Hosaka H, Matsuda M, Okamura-Ikeda K, Motokawa Y, Suzuki M . Crystal structure of bovine lipoyltransferase in complex with lipoyl-AMP. J Mol Biol. 2007; 371(1):222-34. DOI: 10.1016/j.jmb.2007.05.059. View

20.

Reed L, Koike M, LEVITCH M, Leach F . Studies on the nature and reactions of protein-bound lipoic acid. J Biol Chem. 1958; 232(1):143-58. View