2c0h
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X-RAY STRUCTURE OF BETA-MANNANASE FROM BLUE MUSSEL MYTILUS EDULIS
OverviewOverview
Endo-beta-1,4-d-mannanase is the key depolymerizing enzyme for, beta-1,4-mannan polymers present in the cell walls of plants and some, algae, as well as in some types of plant seeds. Endo-1,4-beta-mannanase, from blue mussel Mytilus edulis (MeMan5A) belongs to the glycoside, hydrolase (GH) family 5 enzymes. The MeMan5A structure has been determined, to 1.6A resolution using the multiple-wavelength anomalous dispersion, method at the selenium K edge with selenomethionyl MeMan5A expressed in, the yeast Pichia pastoris. As expected for GH 5 enzymes, the structure, showed a (betaalpha)(8)-barrel fold. An unusually large number of, histidine side-chains are exposed on the surface, which may relate to its, location within the crystalline style of the digestive tract of the, mussel. Kinetic ... [(full description)]
About this StructureAbout this Structure
2C0H is a [Single protein] structure of sequence from [Mytilus edulis] with SO4 as [ligand]. Active as [Mannan endo-1,4-beta-mannosidase], with EC number [3.2.1.78]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
ReferenceReference
Three-dimensional crystal structure and enzymic characterization of beta-mannanase Man5A from blue mussel Mytilus edulis., Larsson AM, Anderson L, Xu B, Munoz IG, Uson I, Janson JC, Stalbrand H, Stahlberg J, J Mol Biol. 2006 Apr 14;357(5):1500-10. Epub 2006 Jan 31. PMID:16487541
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