3UW0
Pectin methylesterase from Yersinia enterocolitica
Summary for 3UW0
| Entry DOI | 10.2210/pdb3uw0/pdb |
| Descriptor | pectinesterase (2 entities in total) |
| Functional Keywords | right-handed beta-helix, carbohydrate esterase, hydrolase |
| Biological source | Yersinia enterocolitica subsp. enterocolitica |
| Total number of polymer chains | 1 |
| Total formula weight | 39784.46 |
| Authors | Abbott, D.W.,Boraston, A.B. (deposition date: 2011-11-30, release date: 2012-02-08, Last modification date: 2023-09-13) |
| Primary citation | Boraston, A.B.,Abbott, D.W. Structure of a pectin methylesterase from Yersinia enterocolitica. Acta Crystallogr.,Sect.F, 68:129-133, 2012 Cited by PubMed Abstract: Pectin methylesterases (PMEs) are family 8 carbohydrate esterases (CE8s) which remove the methyl group from methylesterified galacturonic acid (GalA) residues within pectin. Although the role of pectinases such as PMEs within dedicated phytopathogens has been well established, the significance of homologous enzymes found within the genomes of human enteropathogens remains to be determined. Presented here is the low-resolution (3.5 Å) structure of the CE8 from Yersinia enterocolitica (YeCE8). The high degree of structural conservation in the topology of the active-site cleft and catalytic apparatus that is shared with a characterized PME from a bacterial phytopathogen (i) indicates that YeCE8 is active on methylated pectin and (ii) highlights a more prominent role for pectin utilization in Yersinia than in other enteropathogenic species. PubMed: 22297983DOI: 10.1107/S1744309111055400 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.5 Å) |
Structure validation
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