Characterization of a novel pectate lyase, Pel10A, from Pseudomonas cellulosa.
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 P2(1), with unit-cell parameters a = 47.7, b = 106.1, c = 55.4 A, beta = 92.0 degrees, and have two molecules in the asymmetric unit. The crystals diffract beyond 1.5 A using synchrotron radiation.
Charnock
S J
SJ
Structural Biology Laboratory, Department of Chemistry, University of York, Heslington, York YO10 5DD, England.
Brown
I E
IE
Turkenburg
J P
JP
Black
G W
GW
Davies
G J
GJ
D003460:Crystallization; D018360:Crystallography, X-Ray; D004926:Escherichia coli; D011133:Polysaccharide-Lyases / Q000737:chemistry* / Q000378:metabolism; D011487:Protein Conformation; D011549:Pseudomonas / Q000201:enzymology*; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism
D011994:Recombinant Proteins; D011133:Polysaccharide-Lyases; C426004:pectate lyase 10A