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Structure paper

TitleCrystal structure of firefly luciferase in a second catalytic conformation supports a domain alternation mechanism.
Journal, issue, pagesBiochemistry, Vol. 51, Page 6493-6495, Year 2012
Publish dateJul 13, 2012 (structure data deposition date)
AuthorsSundlov, J.A. / Fontaine, D.M. / Southworth, T.L. / Branchini, B.R. / Gulick, A.M.
External linksBiochemistry / PubMed:22852753
MethodsX-ray diffraction
Resolution2.396 - 2.624 Å
Structure data

PDB-4g36:
Photinus pyralis luciferase in the adenylate-forming conformation bound to DLSA
Method: X-RAY DIFFRACTION / Resolution: 2.624 Å

PDB-4g37:
Structure of cross-linked firefly luciferase in second catalytic conformation
Method: X-RAY DIFFRACTION / Resolution: 2.396 Å

Chemicals

ChemComp-SLU:
5'-O-[N-(DEHYDROLUCIFERYL)-SULFAMOYL] ADENOSINE

ChemComp-HOH:
WATER

ChemComp-XLX:
4,4'-(ethylenediimino)bis[4-oxobutyrate]

ChemComp-SO4:
SULFATE ION

ChemComp-CL:
Unknown entry

Source
  • photinus pyralis (common eastern firefly)
KeywordsLIGASE / ANL Superfamily / adenylating enzymes / luciferase / domain alternation / firefly luciferase / trapped conformation / chemical cross-linker

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