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Structure paper

TitleCatalysis Uncoupling in a Glutamine Amidotransferase Bienzyme by Unblocking the Glutaminase Active Site.
Journal, issue, pagesChem. Biol., Vol. 19, Page 1589-, Year 2012
Publish dateJun 2, 2009 (structure data deposition date)
AuthorsList, F. / Vega, M.C. / Razeto, A. / Hager, M.C. / Sterner, R. / Wilmanns, M.
External linksChem. Biol. / PubMed:23261602
MethodsX-ray diffraction
Resolution2.41 - 2.601 Å
Structure data

PDB-2wjz:
Crystal structure of (HisH) K181A Y138A mutant of imidazoleglycerolphosphate synthase (HisH HisF) which displays constitutive glutaminase activity
Method: X-RAY DIFFRACTION / Resolution: 2.601 Å

PDB-3zr4:
STRUCTURAL EVIDENCE FOR AMMONIA TUNNELING ACROSS THE (BETA-ALPHA)8 BARREL OF THE IMIDAZOLE GLYCEROL PHOSPHATE SYNTHASE BIENZYME COMPLEX
Method: X-RAY DIFFRACTION / Resolution: 2.41 Å

Chemicals

ChemComp-PO4:
PHOSPHATE ION

ChemComp-HOH:
WATER

ChemComp-GOL:
GLYCEROL

ChemComp-GLN:
GLUTAMINE

Source
  • thermotoga maritima (bacteria)
KeywordsLYASE/TRANSFERASE / LYASE-TRANSFERASE COMPLEX / AMINO-ACID BIOSYNTHESIS / AMMONIA CHANNEL / HISTIDINE BIOSYNTHESIS / CYCLASE / GLUTAMINASE / TRANSFERASE

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