3h3k

Structure of A. acidocaldarius cellulase CelA in complex with cellotetraose

spinqualitylabelsall models 3h3k, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3h3k is a 1 chain structure with sequence from Alicyclobacillus acidocaldarius subsp. acidocaldarius. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.1Å Ligands: BGC, CA, GLC, MPD, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q9AJS0_ALIAC 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 Alicyclobacillus acidocaldarius endoglucanase Cel9A (AaCel9A) is an inverting glycoside hydrolase with beta-1,4-glucanase activity on soluble polymeric substrates. Here, we report three X-ray structures of AaCel9A: a ligand-free structure at 1.8 A resolution and two complexes at 2.66 and 2.1 A resolution, respectively, with cellobiose obtained by co-crystallization and with cellotetraose obtained by the soaking method. AaCel9A forms an (alpha/alpha)(6)-barrel like other glycoside hydrolase family 9 enzymes. When cellobiose is used as a ligand, three glucosyl binding subsites are occupied, including two on the glycone side, while with cellotetraose as a ligand, five subsites, including four on the glycone side, are occupied. A structural comparison showed no conformational rearrangement of AaCel9A upon ligand binding. The structural analysis demonstrates that of the four minus subsites identified, subsites -1 and -2 show the strongest interaction with bound glucose. In conjunction with the open active-site cleft of AaCel9A, this is able to reconcile the previously observed cleavage of short-chain oligosaccharides with cellobiose as main product with the endo mode of action on larger polysaccharides. Crystal structures of A. acidocaldarius endoglucanase Cel9A in complex with cello-oligosaccharides: strong -1 and -2 subsites mimic cellobiohydrolase activity.,Eckert K, Vigouroux A, Lo Leggio L, Morera S J Mol Biol. 2009 Nov 20;394(1):61-70. Epub 2009 Aug 31. PMID:19729024 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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