5ITW
Crystal structure of Bacillus subtilis BacC Dihydroanticapsin 7-dehydrogenase
Summary for 5ITW
| Entry DOI | 10.2210/pdb5itw/pdb |
| Related | 5ITV |
| Descriptor | Dihydroanticapsin 7-dehydrogenase, SULFATE ION (3 entities in total) |
| Functional Keywords | oxidoreductase, short-chain dehydrogenases/reductases, rossmann fold, nad(p) binding domain |
| Biological source | Bacillus subtilis (strain 168) |
| Total number of polymer chains | 4 |
| Total formula weight | 110169.68 |
| Authors | Perinbam, K.,Balaram, H.,Row, T.N.G.,Gopal, B. (deposition date: 2016-03-17, release date: 2017-02-22, Last modification date: 2023-11-08) |
| Primary citation | Perinbam, K.,Balaram, H.,Guru Row, T.N.,Gopal, B. Probing the influence of non-covalent contact networks identified by charge density analysis on the oxidoreductase BacC. Protein Eng. Des. Sel., 30:265-272, 2017 Cited by PubMed Abstract: Bacillus subtilis BacC is an oxidoreductase involved in the biosynthesis of the potent antibiotic bacilysin. The crystal structure of BacC was determined at 1.19 Å resolution. An experimental charge density approach was used to calculate non-covalent interactions within the monomer and across the dimeric interface of BacC. This interaction network, in turn, enabled an analysis of non-covalently connected paths that span the protein structure. One of the pathways of non-covalent interactions was examined by mutational analysis. Biochemical analysis of BacC mutants with potential disruptions in non-covalent interactions along this path revealed that residues that form nodes in pathways of non-covalent interactions influence catalytic activity more than others in a similar chemical environment. Furthermore, we note that nodes in the non-covalent interaction networks are co-localized with compensatory mutation sites identified by multiple sequence alignment of proteins with low sequence similarity to BacC. Put together, this analysis supports the hypothesis that non-covalent nodes represent conserved structural features that can impact the catalytic activity of an enzyme. PubMed: 28158843DOI: 10.1093/protein/gzx006 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.19 Å) |
Structure validation
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