3PL0

Crystal structure of a bsmA homolog (Mpe_A2762) from Methylobium petroleophilum PM1 at 1.91 A resolution

Summary for 3PL0

• Entry DOI: 10.2210/pdb3pl0/pdb
• Descriptor: Uncharacterized protein, GLYCEROL, CHLORIDE ION, ... (4 entities in total)
• Functional Keywords: quorum sensing, biofilm formation, double-stranded beta-helix fold, structural genomics, joint center for structural genomics, jcsg, protein structure initiative, psi-biology, biosynthetic protein
• Biological source: Methylibium petroleiphilum
• Total number of polymer chains: 2
• Total formula weight: 57412.49

Authors

Joint Center for Structural Genomics (JCSG) (deposition date: 2010-11-12, release date: 2010-12-08, Last modification date: 2024-11-20)

Primary citation

Xu, Q.,Grant, J.,Chiu, H.J.,Farr, C.L.,Jaroszewski, L.,Knuth, M.W.,Miller, M.D.,Lesley, S.A.,Godzik, A.,Elsliger, M.A.,Deacon, A.M.,Wilson, I.A.
Crystal structure of a member of a novel family of dioxygenases (PF10014) reveals a conserved cupin fold and active site.
Proteins, 82:164-170, 2014

PubMed Abstract: PF10014 is a novel family of 2-oxyglutarate-Fe(2+) -dependent dioxygenases that are involved in biosynthesis of antibiotics and regulation of biofilm formation, likely by catalyzing hydroxylation of free amino acids or other related ligands. The crystal structure of a PF10014 member from Methylibium petroleiphilum at 1.9 Å resolution shows strong structural similarity to cupin dioxygenases in overall fold and active site, despite very remote homology. However, one of the β-strands of the cupin catalytic core is replaced by a loop that displays conformational isomerism that likely regulates the active site.

PubMed: 23852666
DOI: 10.1002/prot.24362

Experimental method

X-RAY DIFFRACTION (1.91 Å)