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Structure paper

TitleDirected evolution of the tryptophan synthase beta-subunit for stand-alone function recapitulates allosteric activation.
Journal, issue, pagesProc. Natl. Acad. Sci. USA, Vol. 112, Page 14599-14604, Year 2015
Publish dateSep 21, 2015 (structure data deposition date)
AuthorsBuller, A.R. / Brinkmann-Chen, S. / Romney, D.K. / Herger, M. / Murciano-Calles, J. / Arnold, F.H.
External linksProc. Natl. Acad. Sci. USA / PubMed:26553994
MethodsX-ray diffraction
Resolution1.69 - 2.76 Å
Structure data

PDB-5dvz:
Holo TrpB from Pyrococcus furiosus
Method: X-RAY DIFFRACTION / Resolution: 1.69 Å

PDB-5dw0:
TrpB from Pyrococcus furiosus with L-serine bound as the external aldimine
Method: X-RAY DIFFRACTION / Resolution: 2.01 Å

PDB-5dw3:
Tryptophan Synthase beta-subunit from Pyrococcus furiosus with product L-tryptophan non-covalently bound in the active site
Method: X-RAY DIFFRACTION / Resolution: 1.74 Å

PDB-5e0k:
X-ray crystal structure of tryptophan synthase complex from Pyrococcus furiosus at 2.76 A
Method: X-RAY DIFFRACTION / Resolution: 2.76 Å

Chemicals

ChemComp-NA:
Unknown entry

ChemComp-PO4:
PHOSPHATE ION

ChemComp-HOH:
WATER

ChemComp-PLS:
[3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YLMETHYL]-SERINE

ChemComp-TRP:
TRYPTOPHAN

Source
  • pyrococcus furiosus (strain atcc 43587 / dsm 3638 / jcm 8422 / vc1) (archaea)
KeywordsLYASE / Type II PLP enzyme / Tryptophan Biosynthesis / EC 4.2.1.20 / PLP / External Aldimine / Pr / Tryptophan synthase / Substrate Bound / Complex / Enzyme

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