4EIB
Crystal Structure of Circular Permuted CBM21 (CP90) Gives Insight into the Altered Selectivity on Carbohydrate Binding.
Summary for 4EIB
| Entry DOI | 10.2210/pdb4eib/pdb |
| Descriptor | Glucoamylase, SULFATE ION, AMMONIUM ION, ... (7 entities in total) |
| Functional Keywords | beta barrel, starch binding, amylose, hydrolase |
| Biological source | Rhizopus oryzae More |
| Total number of polymer chains | 2 |
| Total formula weight | 25464.22 |
| Authors | Stephen, P.,Cheng, K.C.,Lyu, P.C. (deposition date: 2012-04-05, release date: 2012-12-12, Last modification date: 2023-11-08) |
| Primary citation | Stephen, P.,Cheng, K.C.,Lyu, P.C. Crystal structure of circular permuted RoCBM21 (CP90): dimerisation and proximity of binding sites Plos One, 7:e50488-e50488, 2012 Cited by PubMed Abstract: 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. PubMed: 23226294DOI: 10.1371/journal.pone.0050488 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.86 Å) |
Structure validation
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