3FW6
Crystal structure of CelM2, a bifunctional glucanase-xylanase protein from a metagenome library
Summary for 3FW6
| Entry DOI | 10.2210/pdb3fw6/pdb |
| Descriptor | Cellulase, ZINC ION (3 entities in total) |
| Functional Keywords | celm2, glucanase-xyanase, glucanase, xylanase, bifunctional enzyme, hydrolase |
| Biological source | uncultured bacterium |
| Total number of polymer chains | 1 |
| Total formula weight | 58367.20 |
| Authors | Hwang, K.Y.,Nam, K.H. (deposition date: 2009-01-17, release date: 2009-03-03, Last modification date: 2023-11-01) |
| Primary citation | Nam, K.H.,Kim, S.-J.,Hwang, K.Y. Crystal structure of CelM2, a bifunctional glucanase-xylanase protein from a metagenome library Biochem.Biophys.Res.Commun., 383:183-186, 2009 Cited by PubMed Abstract: Degradation of polysaccharides by cellulases and xylanases plays an important role in the carbon cycle, but only occurs in plant cell walls, a few bacteria and some animals. This process is also critical in processes such as biomass degradation and fuel production in the conversion cycles of cellulosic biomass. The enzyme CelM2 is bifunctional, because it is able to effectively hydrolyze barley glucan and xylan. Here, we show the crystal structure of the bifunctional enzyme CelM2, isolated from a metagenome library, and describe the sequence information and structure of its two domains. We believe that CelM2 is attractive as an industrial enzyme and that the structural results presented herein provide insights that are relevant to the genetic engineering of multifunctional enzymes. PubMed: 19345197DOI: 10.1016/j.bbrc.2009.03.149 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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