4eib | pdb_00004eib

Crystal Structure of Circular Permuted CBM21 (CP90) Gives Insight into the Altered Selectivity on Carbohydrate Binding.

spinqualitylabelsall models 4eib, resolution 1.86Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4eib is a 2 chain structure with sequence from Rhizopus arrhizus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.86Å Ligands: ACT, CL, NA, NH4, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function B7XC04_RHIOR Publication Abstract from PubMed Glucoamylases, containing starch-binding domains (SBD), have a wide range of scientific and industrial applications. Random mutagenesis and DNA shuffling of the gene encoding a starch-binding domain have resulted in only minor improvements in the affinities of the corresponding protein to their ligands, whereas circular permutation of the RoCBM21 substantially improved its binding affinity and selectivity towards longer-chain carbohydrates. For the study reported herein, we used a standard soluble ligand (amylose EX-I) to characterize the functional and structural aspects of circularly permuted RoCBM21 (CP90). Site-directed mutagenesis and the analysis of crystal structure reveal the dimerisation and an altered binding path, which may be responsible for improved affinity and altered selectivity of this newly created starch-binding domain. The functional and structural characterization of CP90 suggests that it has significant potential in industrial applications. Crystal structure of circular permuted RoCBM21 (CP90): dimerisation and proximity of binding sites.,Stephen P, Cheng KC, Lyu PC PLoS One. 2012;7(11):e50488. doi: 10.1371/journal.pone.0050488. Epub 2012 Nov 30. PMID:23226294 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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