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TitleImprovement of the thermostability and activity of a pectate lyase by single amino acid substitutions, using a strategy based on melting-temperature-guided sequence alignment.
Journal, issue, pagesAppl. Environ. Microbiol., Vol. 74, Page 1183-1189, Year 2008
Publish dateAug 13, 2007 (structure data deposition date)
AuthorsXiao, Z. / Bergeron, H. / Grosse, S. / Beauchemin, M. / Garron, M.L. / Shaya, D. / Sulea, T. / Cygler, M. / Lau, P.C.
External linksAppl. Environ. Microbiol. / PubMed:18156340
MethodsX-ray diffraction
Resolution1.9 - 2.12 Å
Structure data

PDB-2qxz:
pectate lyase R236F from Xanthomonas campestris
Method: X-RAY DIFFRACTION / Resolution: 2.12 Å

PDB-2qy1:
pectate lyase A31G/R236F from Xanthomonas campestris
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

Chemicals

ChemComp-PO4:
PHOSPHATE ION

ChemComp-HOH:
WATER

Source
  • xanthomonas campestris pv. campestris (bacteria)
KeywordsLYASE / pectate lyase / GAG lyase

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