2eqd | pdb_00002eqd

Crystal structure of Cel44A, GH family 44 endoglucanase from Clostridium thermocellum

spinqualitylabelsall models 2eqd, resolution 2.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2eqd is a 1 chain structure with sequence from Clostridium thermocellum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CA, CE8, CL, GOL, ZN Related: 2e4t, 2e0p, 2eex, 2ej1, 2e07 Gene: celJ, celJ-cel44A (Clostridium thermocellum) Resources: FirstGlance, OCA, RCSB, PDBsum 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 crystal structure of Cel44A, which is one of the enzymatic components of the cellulosome of Clostridium thermocellum, was solved at a resolution of 0.96 A. This enzyme belongs to glycoside hydrolase family (GH family) 44. The structure reveals that Cel44A consists of a TIM-like barrel domain and a beta-sandwich domain. The wild-type and the E186Q mutant structures complexed with substrates suggest that two glutamic acid residues, Glu(186) and Glu(359), are the active residues of the enzyme. Biochemical experiments were performed to confirm this idea. The structural features indicate that GH family 44 belongs to clan GH-A and that the reaction catalyzed by Cel44A is retaining type hydrolysis. The stereochemical course of hydrolysis was confirmed by a (1)H NMR experiment using the reduced cellooligosaccharide as a substrate. Crystal structure of Cel44A, a glycoside hydrolase family 44 endoglucanase from Clostridium thermocellum.,Kitago Y, Karita S, Watanabe N, Kamiya M, Aizawa T, Sakka K, Tanaka I J Biol Chem. 2007 Dec 7;282(49):35703-11. Epub 2007 Sep 28. PMID:17905739 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Glucanase

Proteopedia Page Contributors and Editors (what is this?)

OCA