1BHE

POLYGALACTURONASE FROM ERWINIA CAROTOVORA SSP. CAROTOVORA

Summary for 1BHE

• Entry DOI: 10.2210/pdb1bhe/pdb
• Descriptor: POLYGALACTURONASE (2 entities in total)
• Functional Keywords: family 28 glycosyl hydrolase, hydrolyses polygalacturonic acid, glycosidase
• Biological source: Pectobacterium carotovorum subsp. carotovorum
• Cellular location: Secreted: P26509
• Total number of polymer chains: 1
• Total formula weight: 40135.22

Authors

Pickersgill, R.,Smith, D.,Worboys, K.,Jenkins, J. (deposition date: 1998-06-05, release date: 1998-11-11, Last modification date: 2024-11-06)

Primary citation

Pickersgill, R.,Smith, D.,Worboys, K.,Jenkins, J.
Crystal structure of polygalacturonase from Erwinia carotovora ssp. carotovora.
J.Biol.Chem., 273:24660-24664, 1998

PubMed Abstract: 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.

PubMed: 9733763
DOI: 10.1074/jbc.273.38.24660

Experimental method

X-RAY DIFFRACTION (1.9 Å)