1998
DOI: 10.1074/jbc.273.38.24660
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Crystal Structure of Polygalacturonase from Erwinia carotovora ssp. carotovora

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 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 between these t… Show more

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Cited by 172 publications
(154 citation statements)
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“…33). The ␤-sheet PB2a, starting from the sixth turn of the ␤-helix, is typical of PGs and is absent in other proteins sharing the same overall fold (34). The length of the ␤-strands is generally short (3 to 5 residues); more variable is the length of the turns (T) between ␤-strands.…”
Section: Resultsmentioning
confidence: 99%
See 1 more Smart Citation
“…33). The ␤-sheet PB2a, starting from the sixth turn of the ␤-helix, is typical of PGs and is absent in other proteins sharing the same overall fold (34). The length of the ␤-strands is generally short (3 to 5 residues); more variable is the length of the turns (T) between ␤-strands.…”
Section: Resultsmentioning
confidence: 99%
“…1b). This finding is of some interest in view of the polyanionic nature of the substrate and the fact that bacterial pectate lyases and PGs are generally richer in basic amino acids (34,41). It is well known that fungal PGs interact with and are inhibited by plant inhibitors named PGIPs.…”
Section: Discussionmentioning
confidence: 99%
“…By careful inspection of the Hbonding pattern, B2 may be considered a single sheet formed by the clustering of four shorter sheets that interact together. The presence of the additional sheet B2 places the fold of PGIP2 between the typical LRR structure and the ␤-helical architecture found in pectate lyases and PGs that contain three to four ␤-sheets (30)(31)(32)(33). PGIP2 belongs to the plant-specific LRR subfamily characterized by the consensus sequence Lt͞sGxIP in the region following the conserved ''␤-structure ϩ Asn-ladder'' (23).…”
Section: Resultsmentioning
confidence: 99%
“…It may be interesting to speculate at the reasons behind this at the molecular level. Aspartate residue is implicated in the active site of pectinases as a conserved residue [22]. It is noteworthy that a recent paper indicates that carboxyl groups are an essential group for chitinase from A fumigatus [13].…”
Section: Resultsmentioning
confidence: 99%