3PE7
Oligogalacturonate lyase in complex with manganese
Summary for 3PE7
| Entry DOI | 10.2210/pdb3pe7/pdb |
| Descriptor | Oligogalacturonate lyase, MANGANESE (II) ION, CALCIUM ION, ... (5 entities in total) |
| Functional Keywords | seven-bladed beta-propeller, lyase |
| Biological source | Yersinia enterocolitica subsp. enterocolitica |
| Total number of polymer chains | 1 |
| Total formula weight | 44514.52 |
| Authors | Abbott, D.W.,Gilbert, H.J.,Boraston, A.B. (deposition date: 2010-10-25, release date: 2010-11-03, Last modification date: 2023-09-06) |
| Primary citation | Abbott, D.W.,Gilbert, H.J.,Boraston, A.B. The active site of oligogalacturonate lyase provides unique insights into cytoplasmic oligogalacturonate beta-elimination. J.Biol.Chem., 285:39029-39038, 2010 Cited by PubMed Abstract: Oligogalacturonate lyases (OGLs; now also classified as pectate lyase family 22) are cytoplasmic enzymes found in pectinolytic members of Enterobacteriaceae, such as the enteropathogen Yersinia enterocolitica. OGLs utilize a β-elimination mechanism to preferentially catalyze the conversion of saturated and unsaturated digalacturonate into monogalacturonate and the 4,5-unsaturated monogalacturonate-like molecule, 5-keto-4-deoxyuronate. To provide mechanistic insights into the specificity of this enzyme activity, we have characterized the OGL from Y. enterocolitica, YeOGL, on oligogalacturonides and determined its three-dimensional x-ray structure to 1.65 Å. The model contains a Mn(2+) atom in the active site, which is coordinated by three histidines, one glutamine, and an acetate ion. The acetate mimics the binding of the uronate group of galactourono-configured substrates. These findings, in combination with enzyme kinetics and metal supplementation assays, provide a framework for modeling the active site architecture of OGL. This enzyme appears to contain a histidine for the abstraction of the α-proton in the -1 subsite, a residue that is highly conserved throughout the OGL family and represents a unique catalytic base among pectic active lyases. In addition, we present a hypothesis for an emerging relationship observed between the cellular distribution of pectate lyase folding and the distinct metal coordination chemistries of pectate lyases. PubMed: 20851883DOI: 10.1074/jbc.M110.153981 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.65 Å) |
Structure validation
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