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Structure paper

TitleDirected Evolution Mimics Allosteric Activation by Stepwise Tuning of the Conformational Ensemble.
Journal, issue, pagesJ. Am. Chem. Soc., Vol. 140, Page 7256-7266, Year 2018
Publish dateApr 26, 2017 (structure data deposition date)
AuthorsBuller, A.R. / van Roye, P. / Cahn, J.K.B. / Scheele, R.A. / Herger, M. / Arnold, F.H.
External linksJ. Am. Chem. Soc. / PubMed:29712420
MethodsX-ray diffraction
Resolution1.47 - 2.09 Å
Structure data

PDB-5vm5:
Engineered tryptophan synthase b-subunit from Pyrococcus furiosus, PfTrpB2B9, with Ser bound
Method: X-RAY DIFFRACTION / Resolution: 1.67 Å

PDB-6am7:
Engineered tryptophan synthase b-subunit from Pyrococcus furiosus, PfTrpB2B9
Method: X-RAY DIFFRACTION / Resolution: 1.47 Å

PDB-6am8:
Engineered tryptophan synthase b-subunit from Pyrococcus furiosus, PfTrpB2B9 with Trp bound as E(Aex2)
Method: X-RAY DIFFRACTION / Resolution: 1.83 Å

PDB-6am9:
Engineered tryptophan synthase b-subunit from Pyrococcus furiosus, PfTrpB2B9, with Ser-bound in a predominantly closed state.
Method: X-RAY DIFFRACTION / Resolution: 2.09 Å

PDB-6amc:
Engineered tryptophan synthase b-subunit from Pyrococcus furiosus, PfTrpB4D11
Method: X-RAY DIFFRACTION / Resolution: 1.93 Å

PDB-6amh:
Engineered tryptophan synthase b-subunit from Pyrococcus furiosus, PfTrpB4D11 with Ser bound as E(Aex1)
Method: X-RAY DIFFRACTION / Resolution: 1.63 Å

PDB-6ami:
Engineered tryptophan synthase b-subunit from Pyrococcus furiosus, PfTrpB4D11 with Trp non-covalently bound
Method: X-RAY DIFFRACTION / Resolution: 1.97 Å

Chemicals

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

ChemComp-NA:
Unknown entry

ChemComp-0JO:
2-{[(E)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene]amino}prop-2-enoic acid

ChemComp-HOH:
WATER

ChemComp-PO4:
PHOSPHATE ION

ChemComp-TRP:
TRYPTOPHAN

ChemComp-PLT:
[3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YLMETHYL]-L-TRYPTOPHANE

Source
  • pyrococcus furiosus (strain atcc 43587 / dsm 3638 / jcm 8422 / vc1) (archaea)
KeywordsLYASE / PLP / non-canonical amino acid / directed evolution / allostery / BIOSYNTHETIC PROTEIN / PLP Type II / Tryptophan Synthase / Engineered

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