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Structure paper

TitleRole of arginine-304 in the diphosphate-triggered active site closure mechanism of trichodiene synthase.
Journal, issue, pagesBiochemistry, Vol. 44, Page 12719-12727, Year 2005
Publish dateJul 22, 2005 (structure data deposition date)
AuthorsVedula, L.S. / Cane, D.E. / Christianson, D.W.
External linksBiochemistry / PubMed:16171386
MethodsX-ray diffraction
Resolution2.5 - 2.9 Å
Structure data

PDB-2aek:
R304K trichodiene synthase
Method: X-RAY DIFFRACTION / Resolution: 2.9 Å

PDB-2ael:
R304K Trichodiene Synthase: Complex With Mg, Pyrophosphate, and (4R)-7-Azabisabolene
Method: X-RAY DIFFRACTION / Resolution: 2.5 Å

PDB-2aet:
R304K trichodiene synthase: Complex with Mg, pyrophosphate, and (4S)-7-azabisabolene
Method: X-RAY DIFFRACTION / Resolution: 2.75 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-HOH:
WATER

ChemComp-SAZ:
(1S)-N,4-DIMETHYL-N-(4-METHYLPENT-3-ENYL)CYCLOHEX-3-ENAMINIUM

ChemComp-POP:
PYROPHOSPHATE 2-

Source
  • fusarium sporotrichioides (fungus)
KeywordsLYASE / TERPENOID CYCLASE FOLD / SITE-DIRECTED MUTANT / PYROPHOSPHATE / (4R)-7-AZABISABOLENE / terpenoid synthase fold / site-directed mutagenesis / (4S)-7-azabisabolene

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