Characterization of a novel pectate lyase, Pel10A, from Pseudomonas cellulosa

Simon Charnock, Ian E. Brown, Johan Turkenburg, Gary Black, Gideon Davies

Research output: Contribution to journalArticlepeer-review

9 Citations (Scopus)

Abstract

Biological recycling of plant material is essential for biosphere maintenance. This perpetual task involves a complex array of enzymes, including extracellular polysaccharide hydrolases and lyases. Whilst much is known about the structure and function of the hydrolases, relatively little is known about the structures and mechanisms of the corresponding lyases. To this end, crystals of the catalytic module of a novel family 10 pectate lyase, Pel10A from Pseudomonas cellulosa, were obtained using polyethylene glycol 2000 monomethylether as a precipitant. They belong to space group P21, with unit-cell parameters a = 47.7, b = 106.1, c = 55.4 Å, β = 92.0°, and have two molecules in the asymmetric unit. The crystals diffract beyond 1.5 Å using synchrotron radiation.
Original languageEnglish
Pages (from-to)1141-1143
JournalActa Crystallographica Section D: Biological Crystallography
Volume57
Issue number8
DOIs
Publication statusPublished - 2001

Fingerprint Dive into the research topics of 'Characterization of a novel pectate lyase, Pel10A, from Pseudomonas cellulosa'. Together they form a unique fingerprint.

Cite this