9VKM

Crystal structure of the Fe(II)/alpha-ketoglutarate dependent dioxygenase MicC

Summary for 9VKM

• Entry DOI: 10.2210/pdb9vkm/pdb
• Descriptor: Alpha-ketoglutarate-dependent non-heme iron oxygenase MicC Chain A, GLYCEROL, 1,2-ETHANEDIOL, ... (5 entities in total)
• Functional Keywords: oxidoreductase, alpha-ketoglutarate-dependent enzyme, ripp biosynthesis
• Biological source: Mucilaginibacter inviolabilis
• Total number of polymer chains: 2
• Total formula weight: 67936.84

Authors

Guo, S.J. (deposition date: 2025-06-23, release date: 2026-04-29)

Primary citation

Guo, S.,Ma, S.,Song, L.,Wang, J.,Liu, T.,Yan, W.,Zhang, W.,Deng, Z.,Ding, W.,Zhang, Q.
A ribosomally synthesized and posttranslationally modified peptide with ADP-ribosylation.
Proc.Natl.Acad.Sci.USA, 123:e2527653123-e2527653123, 2026

PubMed Abstract: Ribosomally synthesized and posttranslationally modified peptides (RiPPs) are a fertile ground for uncovering new enzymatic chemistry and structural complexity. Here, we describe minviopeptin, an unusual ADP-ribosylated triceptide accessed through heterologous expression of a cryptic biosynthetic gene cluster. Structural and functional analyses reveal a combination of crosslinking, ADP-ribosylation, and oxidative peptide cleavage, underscoring the capacity of RiPP pathways to generate densely functionalized molecular scaffolds. By revealing ADP-ribosylation as a previously unrecognized RiPP modification and exposing reactivity within radical SAM and nonheme iron enzymes, this work broadens the landscape of RiPP biosynthetic chemistries and offers opportunities for natural product diversification and peptide engineering.

PubMed: 41671188
DOI: 10.1073/pnas.2527653123

Experimental method

X-RAY DIFFRACTION (2.2 Å)