Pectate lyase is responsible for the maceration and soft-rotting of plant tissue. It catalyses the eliminative cleavage of pectate to produce oligosaccharides with 4-deoxy-alpha-D-gluc-4-enuronosyl groups at their non-reducing ends. Pectate lyase is an extracellular enzyme and is induced by pectin. It is subject to self-catabolite repression, and has been implicated in plant disease.
The structure and the folding kinetics of one member of this family, pectate lyase C
(pelC)1 from Erwinia chrysanthemi has been investigated in some detail [1]. PelC contains a parallel beta-helix folding motif. The majority of the regular secondary structure is composed of parallel beta-sheets (about
30%). The individual strands of the sheets are connected by unordered loops of varying length. The backbone is then formed by a large helix composed of beta-sheets. There are two disulphide bonds in pelC and 12 proline residues. One of these prolines, Pro220, is involved in a cis peptide bond. he folding mechanism of pelC involves two slow phases that have been attributed to proline isomerization.
Kamen DE, Woody RW.
Folding kinetics of the protein pectate lyase C reveal fast-forming intermediates and slow proline isomerization.
Biochemistry 41 4713-23 2002
[PubMed: 11926834] http://dx.doi.org/10.1021/bi0115129
Akita M, Suzuki A, Kobayashi T, Ito S, Yamane T.
The first structure of pectate lyase belonging to polysaccharide lyase family 3.
Acta Crystallogr. D Biol. Crystallogr. 57 2001 1786-92
[PubMed: 11717490] http://dx.doi.org/10.1107/S0907444901014482
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