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Crystal Structure of Polygalacturonase fromErwinia carotovorassp.carotovora
1998
Journal of Biological Chemistry
The crystal structure of the 40-kDa endo-polygalacturonase from Erwinia carotovora ssp. carotovora was solved by multiple isomorphous replacement and refined at 1.9 Å to a conventional crystallographic R-factor of 0.198 and R free of 0.239. This is the first structure of a polygalacturonase and comprises a 10 turn righthanded parallel -helix domain with two loop regions forming a "tunnel like" substrate-binding cleft. Sequence conservation indicates that the active site of polygalacturonase is
doi:10.1074/jbc.273.38.24660
pmid:9733763
fatcat:qc4ochovkzdtnchvlkpcofmtqm