| Structural highlights
2cn3 is a 2 chain structure with sequence from "ruminiclostridium_thermocellum"_yutin_and_galperin_2013 "ruminiclostridium thermocellum" yutin and galperin 2013. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Ligands: | , , , , |
| Related: | 2cn2 |
| Activity: | Xyloglucan-specific endo-beta-1,4-glucanase, with EC number 3.2.1.151 |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
[XG74_CLOTM] Hydrolyzes the glucosidic bonds of unbranched Glc residues in tamarind seed xyloglucan, producing XXXG, XLXG, XXLG and XLLG. Has low activity on carboxymethylcellulose, lichenan,hydroxyethylcellulose and glucuronoxylan, and no activity on xylan, polygalaturonic acid, wheat arabinoxylan, rhamnogalacturan, curdlan, laminarin, galactomannan, galactan, arabinan and pachyman or amorphous cellulose.[1] [2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The enzymatic degradation of the plant cell wall is central both to the natural carbon cycle and, increasingly, to environmentally friendly routes to biomass conversion, including the production of biofuels. The plant cell wall is a complex composite of cellulose microfibrils embedded in diverse polysaccharides collectively termed hemicelluloses. Xyloglucan is one such polysaccharide whose hydrolysis is catalyzed by diverse xyloglucanases. Here we present the structure of the Clostridium thermocellum xyloglucanase Xgh74A in both apo and ligand-complexed forms. The structures, in combination with mutagenesis data on the catalytic residues and the kinetics and specificity of xyloglucan hydrolysis reveal a complex subsite specificity accommodating seventeen monosaccharide moieties of the multibranched substrate in an open substrate binding terrain.
Crystal structures of Clostridium thermocellum xyloglucanase, XGH74A, reveal the structural basis for xyloglucan recognition and degradation.,Martinez-Fleites C, Guerreiro CI, Baumann MJ, Taylor EJ, Prates JA, Ferreira LM, Fontes CM, Brumer H, Davies GJ J Biol Chem. 2006 Aug 25;281(34):24922-33. Epub 2006 Jun 13. PMID:16772298[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Zverlov VV, Schantz N, Schmitt-Kopplin P, Schwarz WH. Two new major subunits in the cellulosome of Clostridium thermocellum: xyloglucanase Xgh74A and endoxylanase Xyn10D. Microbiology. 2005 Oct;151(Pt 10):3395-401. PMID:16207921 doi:http://dx.doi.org/10.1099/mic.0.28206-0
- ↑ Martinez-Fleites C, Guerreiro CI, Baumann MJ, Taylor EJ, Prates JA, Ferreira LM, Fontes CM, Brumer H, Davies GJ. Crystal structures of Clostridium thermocellum xyloglucanase, XGH74A, reveal the structural basis for xyloglucan recognition and degradation. J Biol Chem. 2006 Aug 25;281(34):24922-33. Epub 2006 Jun 13. PMID:16772298 doi:10.1074/jbc.M603583200
- ↑ Martinez-Fleites C, Guerreiro CI, Baumann MJ, Taylor EJ, Prates JA, Ferreira LM, Fontes CM, Brumer H, Davies GJ. Crystal structures of Clostridium thermocellum xyloglucanase, XGH74A, reveal the structural basis for xyloglucan recognition and degradation. J Biol Chem. 2006 Aug 25;281(34):24922-33. Epub 2006 Jun 13. PMID:16772298 doi:10.1074/jbc.M603583200
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