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Structure paper

TitleStructure and Function of a Complex between Chorismate Mutase and Dahp Synthase: Efficiency Boost for the Junior Partner.
Journal, issue, pagesEmbo J., Vol. 28, Page 2128-, Year 2009
Publish dateDec 20, 2007 (structure data deposition date)
AuthorsSasso, S. / Okvist, M. / Roderer, K. / Gamper, M. / Codoni, G. / Krengel, U. / Kast, P.
External linksEmbo J. / PubMed:19556970
MethodsX-ray diffraction
Resolution1.65 - 2.35 Å
Structure data

PDB-2vkl:
X-ray crystal structure of the intracellular Chorismate mutase from Mycobactrerium Tuberculosis in complex with malate
Method: X-RAY DIFFRACTION / Resolution: 1.65 Å

PDB-2w19:
Non-covalent complex between dahp synthase and chorismate mutase from Mycobacterium tuberculosis
Method: X-RAY DIFFRACTION / Resolution: 2.15 Å

PDB-2w1a:
Non-covalent complex between dahp synthase and chorismate mutase from Mycobacterium tuberculosis with bound tsa
Method: X-RAY DIFFRACTION / Resolution: 2.35 Å

Chemicals

ChemComp-MLT:
D-MALATE

ChemComp-HOH:
WATER

ChemComp-GOL:
GLYCEROL

ChemComp-SO4:
SULFATE ION

ChemComp-MN:
Unknown entry

ChemComp-CE1:
O-DODECANYL OCTAETHYLENE GLYCOL

ChemComp-PG4:
TETRAETHYLENE GLYCOL / precipitant*YM

ChemComp-TSA:
8-HYDROXY-2-OXA-BICYCLO[3.3.1]NON-6-ENE-3,5-DICARBOXYLIC ACID

Source
  • mycobacterium tuberculosis (bacteria)
KeywordsISOMERASE / HELICAL / TUBERCULOSIS / INTRACELLULAR / CHORISMATE MUTASE / TRANSFERASE/ISOMERASE / TRANSFERASE-ISOMERASE COMPLEX / TRANSFERASE ISOMERASE COMPLEX / AROMATIC AMINO ACID BIOSYNTHESIS / MULTI-ENZYME COMPLEX / PROTEIN-PROTEIN INTERACTIONS / ENZYME ACTIVATION / FEEDBACK REGULATION / SHIKIMATE PATHWAY / COMPLEX FORMATION / MYCOBACTERIUM TUBERCULOSIS RV0948C / TRANSFERASE / DRUG TARGET / ENZYME CATALYSIS

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