title: 1.37 Å crystal structure of pathogenic factor pectate lyase from Acidovorax citrulli.
abstract: Pectates lyase (Pel) plays an important role in bacteria pathogenicity. The crystal structure of Pel from Acidovorax citrulli (AcPel) has been solved to 1.37 Å resolution. AcPel belongs to the polysaccharide lyase family 1 (PL1), which has a characteristic right-handed β-helix fold. AcPel is similar with other Pels in the PL1 family, but also shows some differences at the substrate binding site.
authors.affiliation: Department of Plant Pathology, China Agricultural University, Beijing, China.
authors.forename: Qun
authors.initials: Q
authors.lastname: Tang
authors.forename: Yan-Ping
authors.initials: YP
authors.lastname: Liu
authors.forename: Zheng-Guang
authors.initials: ZG
authors.lastname: Ren
authors.forename: Xiao-Xue
authors.initials: XX
authors.lastname: Yan
authors.forename: Li-Qun
authors.initials: LQ
authors.lastname: Zhang
mesh_terms: D000595:Amino Acid Sequence; D042621:Comamonadaceae / Q000737:chemistry / Q000201:enzymology*; D018360:Crystallography, X-Ray; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011133:Polysaccharide-Lyases / Q000737:chemistry*; D017433:Protein Structure, Secondary; D016415:Sequence Alignment
chemical_list: D011133:Polysaccharide-Lyases; C023911:pectate lyase
keywords: Acidovorax citrulli; crystal structure; pathogenic factor; pectate lyase; right-handed β-helix