4M7T

Crystal structure of BtrN in complex with AdoMet and 2-DOIA

Summary for 4M7T

• Entry DOI: 10.2210/pdb4m7t/pdb
• Descriptor: BtrN, IRON/SULFUR CLUSTER, S-ADENOSYLMETHIONINE, ... (6 entities in total)
• Functional Keywords: adomet radical fold, metal binding protein
• Biological source: Bacillus circulans
• Total number of polymer chains: 1
• Total formula weight: 32019.00

Authors

Drennan, C.L.,Goldman, P.J. (deposition date: 2013-08-12, release date: 2013-10-02, Last modification date: 2024-02-28)

Primary citation

Goldman, P.J.,Grove, T.L.,Booker, S.J.,Drennan, C.L.
X-ray analysis of butirosin biosynthetic enzyme BtrN redefines structural motifs for AdoMet radical chemistry.
Proc.Natl.Acad.Sci.USA, 110:15949-15954, 2013

PubMed Abstract: The 2-deoxy-scyllo-inosamine (DOIA) dehydrogenases are key enzymes in the biosynthesis of 2-deoxystreptamine-containing aminoglycoside antibiotics. In contrast to most DOIA dehydrogenases, which are NAD-dependent, the DOIA dehydrogenase from Bacillus circulans (BtrN) is an S-adenosyl-l-methionine (AdoMet) radical enzyme. To examine how BtrN employs AdoMet radical chemistry, we have determined its structure with AdoMet and substrate to 1.56 Å resolution. We find a previously undescribed modification to the core AdoMet radical fold: instead of the canonical (β/α)6 architecture, BtrN displays a (β5/α4) motif. We further find that an auxiliary [4Fe-4S] cluster in BtrN, thought to bind substrate, is instead implicated in substrate-radical oxidation. High structural homology in the auxiliary cluster binding region between BtrN, fellow AdoMet radical dehydrogenase anSME, and molybdenum cofactor biosynthetic enzyme MoaA provides support for the establishment of an AdoMet radical structural motif that is likely common to ~6,400 uncharacterized AdoMet radical enzymes.

PubMed: 24048029
DOI: 10.1073/pnas.1312228110

Experimental method

X-RAY DIFFRACTION (1.56 Å)