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TitleThe structures of anthranilate synthase of Serratia marcescens crystallized in the presence of (i) its substrates, chorismate and glutamine, and a product, glutamate, and (ii) its end-product inhibitor, L-tryptophan.
Journal, issue, pagesProc. Natl. Acad. Sci. USA, Vol. 98, Page 6021-6026, Year 2001
Publish dateMar 10, 2001 (structure data deposition date)
AuthorsSpraggon, G. / Kim, C. / Nguyen-Huu, X. / Yee, M.C. / Yanofsky, C. / Mills, S.E.
External linksProc. Natl. Acad. Sci. USA / PubMed:11371633
MethodsX-ray diffraction
Resolution1.95 - 2.4 Å
Structure data

PDB-1i7q:
ANTHRANILATE SYNTHASE FROM S. MARCESCENS
Method: X-RAY DIFFRACTION / Resolution: 1.95 Å

PDB-1i7s:
ANTHRANILATE SYNTHASE FROM SERRATIA MARCESCENS IN COMPLEX WITH ITS END PRODUCT INHIBITOR L-TRYPTOPHAN
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-BEZ:
BENZOIC ACID

ChemComp-PYR:
PYRUVIC ACID

ChemComp-GLU:
GLUTAMIC ACID

ChemComp-HOH:
WATER

ChemComp-TRP:
TRYPTOPHAN

Source
  • serratia marcescens (bacteria)
KeywordsLYASE / ANTHRANILATE SYNTHASE / GLUTAMYL THIOESTER / ANTHRANILATE BIOSYNTHESIS / CHORISMATE BINDING / END PRODUCT INHIBITION / TRYPTOPHAN BINDING / CONFORMATIONAL CHANGE

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