4v17 | pdb_00004v17

Structure of a novel carbohydrate binding module from glycoside hydrolase family 5 glucanase from Ruminococcus flavefaciens FD-1

spinqualitylabelsall models 4v17, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4v17 is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 4v18, 4v1b, 4v1i Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Publication Abstract from PubMed Anaerobic bacteria organize carbohydrate-active enzymes into a multi-component complex, the cellulosome, which degrades cellulose and hemicellulose highly efficiently. Genome sequencing of Ruminococcus flavefaciens FD-1 offers extensive information on the range and diversity of the enzymatic and structural components of the cellulosome. The R. flavefaciens FD-1 genome encodes over 200 dockerin-containing proteins, most of which are of unknown function. One of these modular proteins comprises a glycoside hydrolase family 5 catalytic module (GH5) linked to an unclassified carbohydrate-binding module (CBM-Rf1) and a dockerin. The novel CBM-Rf1 has been purified and crystallized. The crystals belonged to the trigonal space group R32:H. The CBM-Rf1 structure was determined by a multiple-wavelength anomalous dispersion experiment using AutoSol from the PHENIX suite using both selenomethionyl-derivative and native data to resolutions of 2.28 and 2.0 A, respectively. Expression, purification and crystallization of a novel carbohydrate-binding module from the Ruminococcus flavefaciens cellulosome.,Venditto I, Centeno MS, Ferreira LM, Fontes CM, Najmudin S Acta Crystallogr F Struct Biol Commun. 2014 Dec 1;70(Pt 12):1653-6. doi:, 10.1107/S2053230X14024248. Epub 2014 Nov 14. PMID:25484220 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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