Structural highlights
4v20 is a 1 chain structure with sequence from Aspergillus fumigatus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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| Method: | X-ray diffraction, Resolution 1.5Å |
| Ligands: | , , , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
CBHB_ASPFU The biological conversion of cellulose to glucose generally requires three types of hydrolytic enzymes: (1) Endoglucanases which cut internal beta-1,4-glucosidic bonds; (2) Exocellobiohydrolases that cut the dissaccharide cellobiose from the non-reducing end of the cellulose polymer chain; (3) Beta-1,4-glucosidases which hydrolyze the cellobiose and other short cello-oligosaccharides to glucose.
Publication Abstract from PubMed
The enzymatic degradation of plant cell-wall cellulose is central to many industrial processes, including second-generation biofuel production. Key players in this deconstruction are the fungal cellobiohydrolases (CBHs), notably those from family GH7 of the carbohydrate-active enzymes (CAZY) database, which are generally known as CBHI enzymes. Here, three-dimensional structures are reported of the Aspergillus fumigatus CBHI Cel7A solved in uncomplexed and disaccharide-bound forms at resolutions of 1.8 and 1.5 A, respectively. The product complex with a disaccharide in the +1 and +2 subsites adds to the growing three-dimensional insight into this family of industrially relevant biocatalysts.
The three-dimensional structure of the cellobiohydrolase Cel7A from Aspergillus fumigatus at 1.5 A resolution.,Moroz OV, Maranta M, Shaghasi T, Harris PV, Wilson KS, Davies GJ Acta Crystallogr F Struct Biol Commun. 2015 Jan 1;71(Pt 1):114-20. doi:, 10.1107/S2053230X14027307. Epub 2015 Jan 1. PMID:25615982[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Moroz OV, Maranta M, Shaghasi T, Harris PV, Wilson KS, Davies GJ. The three-dimensional structure of the cellobiohydrolase Cel7A from Aspergillus fumigatus at 1.5 A resolution. Acta Crystallogr F Struct Biol Commun. 2015 Jan 1;71(Pt 1):114-20. doi:, 10.1107/S2053230X14027307. Epub 2015 Jan 1. PMID:25615982 doi:http://dx.doi.org/10.1107/S2053230X14027307
