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Structure paper

TitleUncoupling conformational states from activity in an allosteric enzyme.
Journal, issue, pagesNat Commun, Vol. 8, Page 203-203, Year 2017
Publish dateJul 12, 2016 (structure data deposition date)
AuthorsPisco, J.P. / Chiara, C. / Pacholarz, K.J. / Garza-Garcia, A. / Ogrodowicz, R.W. / Walker, P.A. / Barran, P.E. / Smerdon, S.J. / Carvalho, L.P.S.
External linksNat Commun / PubMed:28781362
MethodsX-ray diffraction
Resolution2.02 - 2.0601 Å
Structure data

PDB-5lht:
ATP Phosphoribosyltransferase from Mycobacterium tuberculosis in complex with the allosteric activator 3-(2-Thienyl)-L-alanine
Method: X-RAY DIFFRACTION / Resolution: 2.0601 Å

PDB-5lhu:
ATP Phosphoribosyltransferase from Mycobacterium tuberculosis in complex with the allosteric inhibitor L-Histidine
Method: X-RAY DIFFRACTION / Resolution: 2.02 Å

Chemicals

ChemComp-TIH:
BETA(2-THIENYL)ALANINE

ChemComp-SO4:
SULFATE ION

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

ChemComp-HIS:
HISTIDINE

Source
  • mycobacterium tuberculosis (strain atcc 25618 / h37rv) (bacteria)
KeywordsTRANSFERASE / ATP-PRTase / ACT / His G / Histidine biosynthesis

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