1.37 Å Crystal structure of pathogenic factor pectate lyase from Acidovorax citrulli
| Autor: | Zheng-Guang Ren, Yan-Ping Liu, Xiao-Xue Yan, Li-Qun Zhang, Qun Tang |
|---|---|
| Rok vydání: | 2013 |
| Předmět: |
integumentary system
Acidovorax citrulli Pathogenic factor virus diseases Crystal structure biochemical phenomena metabolism and nutrition Biology biology.organism_classification Pathogenicity Lyase Biochemistry Microbiology immune system diseases Structural Biology hemic and lymphatic diseases Pectate lyase Binding site Molecular Biology Bacteria |
| Zdroj: | Proteins: Structure, Function, and Bioinformatics. 81:1485-1490 |
| ISSN: | 0887-3585 |
| DOI: | 10.1002/prot.24298 |
| Popis: | 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 A 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. |
| Databáze: | OpenAIRE |
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