|SMART accession number:||SM00656|
|Interpro abstract (IPR002022):|
Pectate lyase EC 184.108.40.206 is an enzyme involved in the maceration and soft rotting of plant tissue. Pectate lyase is responsible for the eliminative cleavage of pectate, yielding oligosaccharides with 4-deoxy-alpha-D-mann-4-enuronosyl groups at their non-reducing ends. The protein is maximally expressed late in pollen development. It has been suggested that the pollen expression of pectate lyase genes might relate to a requirement for pectin degradation during pollen tube growth [(PUBMED:1983191)].
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 [(PUBMED:11926834),(PUBMED:8502994)]. 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.
Some of the proteins in this family are allergens. Allergies are hypersensitivity reactions of the immune system to specific substances called allergens (such as pollen, stings, drugs, or food) that, in most people, result in no symptoms. A nomenclature system has been established for antigens (allergens) that cause IgE-mediated atopic allergies in humans [WHO/IUIS Allergen Nomenclature Subcommittee King T.P., Hoffmann D., Loewenstein H., Marsh D.G., Platts-Mills T.A.E., Thomas W. Bull. World Health Organ. 72:797-806(1994)]. This nomenclature system is defined by a designation that is composed of the first three letters of the genus; a space; the first letter of the species name; a space and an arabic number. In the event that two species names have identical designations, they are discriminated from one another by adding one or more letters (as necessary) to each species designation.
The allergens in this family include allergens with the following designations: Amb a 1, Amb a 2, Amb a 3, Cha o 1, Cup a 1, Cry j 1, Jun a 1.
Two of the major allergens in the pollen of short ragweed (Ambrosia artemisiifolia) are Amb aI and Amb aII. The primary structure of Amb aII has been deduced and has been shown to share ~65% sequence identity with the Amb alpha I multigene family of allergens [(PUBMED:1717566)]. Members of the Amb aI/aII family include Nicotiana tabacum (Common tobacco) pectate lyase, which is similar to the deduced amino acid sequences of two pollen-specific pectate lyase genes identified in Solanum lycopersicum (Tomato) (Lycopersicon esculentum) [(PUBMED:1421152)]; Cry jI, a major allergenic glycoprotein of Cryptomeria japonica (Japanese cedar) - the most common pollen allergen in Japan [(PUBMED:7920021)]; and P56 and P59, which share sequence similarity with pectate lyases of plant pathogenic bacteria [(PUBMED:1983191)].
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- Evolution (species in which this domain is found)
- Metabolism (metabolic pathways involving proteins which contain this domain)
- Structure (3D structures containing this domain)
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