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Structure paper

TitleMolecular basis for the allosteric activation mechanism of the heterodimeric imidazole glycerol phosphate synthase complex.
Journal, issue, pagesNat Commun, Vol. 12, Page 2748-2748, Year 2021
Publish dateSep 10, 2020 (structure data deposition date)
AuthorsWurm, J.P. / Sung, S. / Kneuttinger, A.C. / Hupfeld, E. / Sterner, R. / Wilmanns, M. / Sprangers, R.
External linksNat Commun / PubMed:33980881
MethodsX-ray diffraction
Resolution2.06 Å
Structure data

PDB-7ac8:
Molecular basis for the unique allosteric activation mechanism of the heterodimeric imidazole glycerol phosphate synthase complex.
Method: X-RAY DIFFRACTION / Resolution: 2.06 Å

Chemicals

ChemComp-GUO:
[(2R,3S,4R,5R)-5-[4-aminocarbonyl-5-[(E)-[[(2R,3R,4S,5R)-3,4-bis(oxidanyl)-5-(phosphonooxymethyl)oxolan-2-yl]amino]methylideneamino]imidazol-1-yl]-3,4-bis(oxidanyl)oxolan-2-yl]methyl dihydrogen phosphate

ChemComp-GLN:
GLUTAMINE

ChemComp-PO4:
PHOSPHATE ION

ChemComp-HOH:
WATER

Source
  • thermotoga maritima (bacteria)
  • thermotoga maritima (strain atcc 43589 / msb8 / dsm 3109 / jcm 10099) (bacteria)
KeywordsLYASE / Enzyme regulation / Allostery / Ensemble model / conformational changes / HisF / HisH / Imidazole Glycerol Phosphate Synthase / LYASE (4.3.2.10)

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