3PL0 image
Deposition Date 2010-11-12
Release Date 2010-12-08
Last Version Date 2024-11-20
Entry Detail
PDB ID:
3PL0
Title:
Crystal structure of a bsmA homolog (Mpe_A2762) from Methylobium petroleophilum PM1 at 1.91 A resolution
Biological Source:
Source Organism(s):
Expression System(s):
Method Details:
Experimental Method:
Resolution:
1.91 Å
R-Value Free:
0.21
R-Value Work:
0.16
R-Value Observed:
0.17
Space Group:
P 1 21 1
Macromolecular Entities
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:Uncharacterized protein
Gene (Uniprot):Mpe_A2762
Chain IDs:A, B
Chain Length:254
Number of Molecules:2
Biological Source:Methylibium petroleiphilum
Modified Residue
Compound ID Chain ID Parent Comp ID Details 2D Image
MSE A MET SELENOMETHIONINE
Primary Citation
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)
PMID: 23852666 DOI: 10.1002/prot.24362

Abstact

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.

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Chemical

Disease

Primary Citation of related structures
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