1bhe
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POLYGALACTURONASE FROM ERWINIA CAROTOVORA SSP. CAROTOVORA
OverviewOverview
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 A to a conventional crystallographic R-factor of 0.198 and Rfree of 0.239. This is the first structure of a polygalacturonase and comprises a 10 turn right-handed parallel beta-helix domain with two loop regions forming a "tunnel like" substrate-binding cleft. Sequence conservation indicates that the active site of polygalacturonase is between these two loop regions, and comparison of the structure of polygalacturonase with that of rhamnogalacturonase A from Aspergillus aculeatus enables two conserved aspartates, presumed to be catalytic residues, to be identified. An adjacent histidine, in accord with biochemical results, is also seen. A similarity in overall electrostatic properties of the substrate-binding clefts of polygalacturonase and pectate lyase, which bind and cleave the same substrate, polygalacturonic acid, is also revealed.
About this StructureAbout this Structure
1BHE is a Single protein structure of sequence from Pectobacterium carotovorum. Active as Polygalacturonase, with EC number 3.2.1.15 Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of polygalacturonase from Erwinia carotovora ssp. carotovora., Pickersgill R, Smith D, Worboys K, Jenkins J, J Biol Chem. 1998 Sep 18;273(38):24660-4. PMID:9733763
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