1gxo
From Proteopedia
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MUTANT D189A OF FAMILY 10 POLYSACCHARIDE LYASE FROM CELLVIBRIO CELLULOSA IN COMPLEX WITH TRIGALATURONIC ACID
Overview
Enzyme-catalyzed beta-elimination of sugar uronic acids, exemplified by, the degradation of plant cell wall pectins, plays an important role in a, wide spectrum of biological processes ranging from the recycling of plant, biomass through to pathogen virulence. The three-dimensional crystal, structure of the catalytic module of a "family PL-10" polysaccharide, lyase, Pel10Acm from Cellvibrio japonicus, solved at a resolution of 1.3, A, reveals a new polysaccharide lyase fold and is the first example of a, polygalacturonic acid lyase that does not exhibit the "parallel, beta-helix" topology. The "Michaelis" complex of an inactive mutant in, association with the substrate trigalacturonate/Ca2+ reveals the catalytic, machinery harnessed by this polygalacturonate lyase, which displays a, ... [(full description)]
About this Structure
1GXO is a [Single protein] structure of sequence from [Cellvibrio cellulosa] with CA as [ligand]. Active as [[1]], with EC number [4.2.2.2]. Full crystallographic information is available from [OCA].
Reference
Convergent evolution sheds light on the anti-beta -elimination mechanism common to family 1 and 10 polysaccharide lyases., Charnock SJ, Brown IE, Turkenburg JP, Black GW, Davies GJ, Proc Natl Acad Sci U S A. 2002 Sep 17;99(19):12067-72. Epub 2002 Sep 9. PMID:12221284
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