7U5T

Structure of DHQS/EPSPS dimer from Candida albicans Aro1

Summary for 7U5T

• Entry DOI: 10.2210/pdb7u5t/pdb
• EMDB information: 26358
• Descriptor: Pentafunctional AROM polypeptide (1 entity in total)
• Functional Keywords: biosynthetic protein
• Biological source: Candida albicans
• Total number of polymer chains: 2
• Total formula weight: 339192.50

Authors

Quade, B.,Borek, D.,Otwinowski, Z.,Center for Structural Genomics of Infectious Diseases (CSGID) (deposition date: 2022-03-02, release date: 2022-05-04, Last modification date: 2024-02-14)

Primary citation

Stogios, P.J.,Liston, S.D.,Semper, C.,Quade, B.,Michalska, K.,Evdokimova, E.,Ram, S.,Otwinowski, Z.,Borek, D.,Cowen, L.E.,Savchenko, A.
Molecular analysis and essentiality of Aro1 shikimate biosynthesis multi-enzyme in Candida albicans.
Life Sci Alliance, 5:-, 2022

PubMed Abstract: 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.

PubMed: 35512834
DOI: 10.26508/lsa.202101358

Experimental method

ELECTRON MICROSCOPY (3.43 Å)