5ov4 | pdb_00005ov4

Bacillus megaterium porphobilinogen deaminase D82A mutant

spinqualitylabelsall models 5ov4, resolution 2.69Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5ov4 is a 1 chain structure with sequence from Priestia megaterium. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.692Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q8GCA8_PRIMG Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.[ARBA:ARBA00002869][HAMAP-Rule:MF_00260] Publication Abstract from PubMed The enzyme porphobilinogen deaminase (PBGD) is one of the key enzymes in tetrapyrrole biosynthesis. It catalyses the formation of a linear tetrapyrrole from four molecules of the substrate porphobilinogen (PBG). It has a dipyrromethane cofactor (DPM) in the active site which is covalently linked to a conserved cysteine residue through a thioether bridge. The substrate molecules are linked to the cofactor in a stepwise head-to-tail manner during the reaction, which is catalysed by a conserved aspartate residue: Asp82 in the B. megaterium enzyme. Three mutations have been made affecting Asp82 (D82A, D82E and D82N) and their crystal structures have been determined at resolutions of 2.7, 1.8 and 1.9 A, respectively. These structures reveal that whilst the D82E mutant possesses the DPM cofactor, in the D82N and D82A mutants the cofactor is likely to be missing, incompletely assembled or disordered. Comparison of the mutant PBGD structures with that of the wild-type enzyme shows that there are significant domain movements and suggests that the enzyme adopts `open' and `closed' conformations, potentially in response to substrate binding. Structural studies of domain movement in active-site mutants of porphobilinogen deaminase from Bacillus megaterium.,Guo J, Erskine P, Coker AR, Wood SP, Cooper JB Acta Crystallogr F Struct Biol Commun. 2017 Nov 1;73(Pt 11):612-620. doi:, 10.1107/S2053230X17015436. Epub 2017 Oct 30. PMID:29095155 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Porphobilinogen Deaminase

Proteopedia Page Contributors and Editors (what is this?)

OCA