4G36

Photinus pyralis luciferase in the adenylate-forming conformation bound to DLSA

Summary for 4G36

• Entry DOI: 10.2210/pdb4g36/pdb
• Related: 1LCI 2D1S 3IEP 4G37
• Descriptor: Luciferin 4-monooxygenase, 5'-O-[N-(DEHYDROLUCIFERYL)-SULFAMOYL] ADENOSINE (3 entities in total)
• Functional Keywords: anl superfamily, ligase, adenylating enzymes, luciferase, domain alternation, firefly luciferase
• Biological source: Photinus pyralis (North American firefly)
• Cellular location: Peroxisome: P08659
• Total number of polymer chains: 2
• Total formula weight: 123674.03

Authors

Sundlov, J.A.,Branchini, B.R.,Gulick, A.M. (deposition date: 2012-07-13, release date: 2012-08-15, Last modification date: 2023-09-13)

Primary citation

Sundlov, J.A.,Fontaine, D.M.,Southworth, T.L.,Branchini, B.R.,Gulick, A.M.
Crystal structure of firefly luciferase in a second catalytic conformation supports a domain alternation mechanism.
Biochemistry, 51:6493-6495, 2012

PubMed Abstract: Beetle luciferases catalyze a two-step reaction that includes the initial adenylation of the luciferin substrate, followed by an oxidative decarboxylation that ultimately produces light. Evidence for homologous acyl-CoA synthetases supports a domain alternation catalytic mechanism in which these enzymes' C-terminal domain rotates by ~140° to adopt two conformations that are used to catalyze the two partial reactions. While many structures exist of acyl-CoA synthetases in both conformations, to date only biochemical evidence supports domain alternation with luciferase. We have determined the structure of a cross-linked luciferase enzyme that is trapped in the second conformation. This new structure supports the role of the second catalytic conformation and provides insights into the biochemical mechanism of the luciferase oxidative step.

PubMed: 22852753
DOI: 10.1021/bi300934s

Experimental method

X-RAY DIFFRACTION (2.624 Å)