5MJI

Crystal Structure of RosB with bound intermediate OHC-RP (8-demethyl-8-formylriboflavin-5'-phosphate)

Summary for 5MJI

• Entry DOI: 10.2210/pdb5mji/pdb
• Descriptor: BRAMP domain protein, [(2~{S},3~{R},4~{R})-5-[8-methanoyl-7-methyl-2,4-bis(oxidanylidene)-1~{H}-benzo[g]pteridin-10-ium-10-yl]-2,3,4-tris(oxidanyl)pentyl] dihydrogen phosphate (3 entities in total)
• Functional Keywords: flavodoxin-like, roseoflavin, electron transport, flavoprotein
• Biological source: Streptomyces davawensis JCM 4913
• Total number of polymer chains: 1
• Total formula weight: 29371.02

Authors

Konjik, V.,Bruenle, S.,Demmer, U.,Vanselow, A.,Sandhoff, R.,Mack, M.,Ermler, U. (deposition date: 2016-12-01, release date: 2016-12-28, Last modification date: 2024-05-08)

Primary citation

Konjik, V.,Brunle, S.,Demmer, U.,Vanselow, A.,Sandhoff, R.,Ermler, U.,Mack, M.
The Crystal Structure of RosB: Insights into the Reaction Mechanism of the First Member of a Family of Flavodoxin-like Enzymes.
Angew. Chem. Int. Ed. Engl., 56:1146-1151, 2017

PubMed Abstract: 8-demethyl-8-aminoriboflavin-5'-phosphate (AFP) synthase (RosB) catalyzes the key reaction of roseoflavin biosynthesis by forming AFP from riboflavin-5'-phosphate (RP) and glutamate via the intermediates 8-demethyl-8-formylriboflavin-5'-phosphate (OHC-RP) and 8-demethyl-8-carboxylriboflavin-5'-phosphate (HO C-RP). To understand this reaction in which a methyl substituent of an aromatic ring is replaced by an amine we structurally characterized RosB in complex with OHC-RP (2.0 Å) and AFP (1.7 Å). RosB is composed of four flavodoxin-like subunits which have been upgraded with specific extensions and a unique C-terminal arm. It appears that RosB has evolved from an electron- or hydride-transferring flavoprotein to a sophisticated multi-step enzyme which uses RP as a substrate (and not as a cofactor). Structure-based active site analysis was complemented by mutational and isotope-based mass-spectrometric data to propose an enzymatic mechanism on an atomic basis.

PubMed: 27981706
DOI: 10.1002/anie.201610292

Experimental method

X-RAY DIFFRACTION (2 Å)