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6HQV

Pentafunctional AROM Complex from Chaetomium thermophilum

Summary for 6HQV
Entry DOI10.2210/pdb6hqv/pdb
DescriptorPentafunctional AROM polypeptide, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, ZINC ION, ... (7 entities in total)
Functional Keywordsmultifunctional enzyme, shikimate pathway, aromatic amino acid biosynthesis, 3-dehydroquinate synthase, 3-dehydroquinate dehydratase, shikimate dehydrogenase, shikimate kinase, 3-phosphoshikimate 1-carboxyvinyltransferase, 5-enolpyruvylshikimate-3-phosphate synthase, biosynthetic protein
Biological sourceChaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)
Total number of polymer chains2
Total formula weight352942.15
Authors
Arora Verasto, H.,Hartmann, M.D. (deposition date: 2018-09-25, release date: 2020-05-06, Last modification date: 2024-11-13)
Primary citationArora Veraszto, H.,Logotheti, M.,Albrecht, R.,Leitner, A.,Zhu, H.,Hartmann, M.D.
Architecture and functional dynamics of the pentafunctional AROM complex.
Nat.Chem.Biol., 16:973-978, 2020
Cited by
PubMed Abstract: The AROM complex is a multifunctional metabolic machine with ten enzymatic domains catalyzing the five central steps of the shikimate pathway in fungi and protists. We determined its crystal structure and catalytic behavior, and elucidated its conformational space using a combination of experimental and computational approaches. We derived this space in an elementary approach, exploiting an abundance of conformational information from its monofunctional homologs in the Protein Data Bank. It demonstrates how AROM is optimized for spatial compactness while allowing for unrestricted conformational transitions and a decoupled functioning of its individual enzymatic entities. With this architecture, AROM poses a tractable test case for the effects of active site proximity on the efficiency of both natural metabolic systems and biotechnological pathway optimization approaches. We show that a mere colocalization of enzymes is not sufficient to yield a detectable improvement of metabolic throughput.
PubMed: 32632294
DOI: 10.1038/s41589-020-0587-9
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3 Å)
Structure validation

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