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Structure paper

TitleMolecular analysis and essentiality of Aro1 shikimate biosynthesis multi-enzyme in .
Journal, issue, pagesLife Sci Alliance, Vol. 5, Issue 8, Year 2022
Publish dateMay 5, 2022
AuthorsPeter J Stogios / Sean D Liston / Cameron Semper / Bradley Quade / Karolina Michalska / Elena Evdokimova / Shane Ram / Zbyszek Otwinowski / Dominika Borek / Leah E Cowen / Alexei Savchenko /
PubMed AbstractIn the human fungal pathogen , encodes an essential multi-enzyme that catalyses consecutive steps in the shikimate pathway for biosynthesis of chorismate, a precursor to folate and the aromatic ...In the human fungal pathogen , encodes an essential multi-enzyme that catalyses consecutive steps in the shikimate pathway for biosynthesis of chorismate, a precursor to folate and the aromatic amino acids. We obtained the first molecular image of Aro1 that reveals the architecture of all five enzymatic domains and their arrangement in the context of the full-length protein. Aro1 forms a flexible dimer allowing relative autonomy of enzymatic function of the individual domains. Our activity and in cellulo data suggest that only four of Aro1's enzymatic domains are functional and essential for viability of , whereas the 3-dehydroquinate dehydratase (DHQase) domain is inactive because of active site substitutions. We further demonstrate that in , the type II DHQase Dqd1 can compensate for the inactive DHQase domain of Aro1, suggesting an unrecognized essential role for this enzyme in shikimate biosynthesis. In contrast, in and , which do not encode a Dqd1 homolog, Aro1 DHQase domains are enzymatically active, highlighting diversity across species.
External linksLife Sci Alliance / PubMed:35512834 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution1.85 - 4.16 Å
Structure data

26357

7u5s

EMDB-26357, PDB-7u5s:
CryoEM structure of the Candida albicans Aro1 dimer
Method: EM (single particle) / Resolution: 4.16 Å

26358

7u5t

EMDB-26358, PDB-7u5t:
Structure of DHQS/EPSPS dimer from Candida albicans Aro1
Method: EM (single particle) / Resolution: 3.43 Å

26359

7u5u

EMDB-26359, PDB-7u5u:
Structure of the SK/DHQase/DHSD dimer from Candida albicans Aro1
Method: EM (single particle) / Resolution: 3.16 Å

PDB-6c5c:
Crystal structure of the 3-dehydroquinate synthase (DHQS) domain of Aro1 from Candida albicans SC5314 in complex with NADH
Method: X-RAY DIFFRACTION / Resolution: 1.85 Å

PDB-7tbu:
Crystal structure of the 5-enolpyruvate-shikimate-3-phosphate synthase (EPSPS) domain of Aro1 from Candida albicans in complex with shikimate-3-phosphate
Method: X-RAY DIFFRACTION / Resolution: 1.85 Å

PDB-7tbv:
Crystal structure of the shikimate kinase + 3-dehydroquinate dehydratase + 3-dehydroshikimate dehydrogenase domains of Aro1 from Candida albicans
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

Chemicals

ChemComp-NAD:
NICOTINAMIDE-ADENINE-DINUCLEOTIDE / NAD*YM

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-CL:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-TRS:
2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL / pH buffer*YM

ChemComp-S3P:
SHIKIMATE-3-PHOSPHATE

ChemComp-MG:
Unknown entry

ChemComp-GOL:
GLYCEROL

Source
  • candida albicans (yeast)
  • candida albicans (strain sc5314 / atcc mya-2876) (yeast)
  • candida albicans ca6 (yeast)
KeywordsLYASE / chorismate biosynthesis / Structural Genomics / Center for Structural Genomics of Infectious Diseases / CSGID / TRANSFERASE / OXIDOREDUCTASE / BIOSYNTHETIC PROTEIN

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