5YY2

Crystal structure of AsqI with Zn

Summary for 5YY2

Entry DOI	10.2210/pdb5yy2/pdb
Descriptor	Uncharacterized protein AsqI, ZINC ION (3 entities in total)
Functional Keywords	hemocyanin like protein, aspoquinolone biosynthesis, secondary metabolism, metal binding protein
Biological source	Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Total number of polymer chains	1
Total formula weight	85706.03
Authors	Hara, K.,Hashimoto, H.,Kishimoto, S.,Watanabe, K. (deposition date: 2017-12-07, release date: 2018-08-01, Last modification date: 2024-03-27)
Primary citation	Kishimoto, S.,Hara, K.,Hashimoto, H.,Hirayama, Y.,Champagne, P.A.,Houk, K.N.,Tang, Y.,Watanabe, K. Enzymatic one-step ring contraction for quinolone biosynthesis. Nat Commun, 9:2826-2826, 2018 Cited by PubMed Abstract: The 6,6-quinolone scaffolds on which viridicatin-type fungal alkaloids are built are frequently found in metabolites that display useful biological activities. Here we report in vitro and computational analyses leading to the discovery of a hemocyanin-like protein AsqI from the Aspergillus nidulans aspoquinolone biosynthetic pathway that forms viridicatins via a conversion of the cyclopenin-type 6,7-bicyclic system into the viridicatin-type 6,6-bicyclic core through elimination of carbon dioxide and methylamine through methyl isocyanate. PubMed: 30026518 DOI: 10.1038/s41467-018-05221-5 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.91 Å)

Structure validation