3pl0 | pdb_00003pl0

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

spinqualitylabelsall models 3pl0, resolution 1.91Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3pl0 is a 2 chain structure with sequence from Methylibium petroleiphilum PM1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.91Å Ligands: CL, GOL, MSE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A2SJH7_METPP Publication Abstract from PubMed 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 A resolution shows strong structural similarity to cupin dioxygenases in overall fold and active site, despite very remote homology. However, one of the beta-strands of the cupin catalytic core is replaced by a loop that displays conformational isomerism that likely regulates the active site. Crystal structure of a member of a novel family of dioxygenases (PF10014) reveals a conserved cupin fold and active site.,Xu Q, Grant J, Chiu HJ, Farr CL, Jaroszewski L, Knuth MW, Miller MD, Lesley SA, Godzik A, Elsliger MA, Deacon AM, Wilson IA Proteins. 2014 Jan;82(1):164-70. doi: 10.1002/prot.24362. Epub 2013 Sep 10. PMID:23852666 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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