4U9E
Crystal structure of the Zn-directed tetramer of the engineered cyt cb562 variant, A104/57G AB3
Summary for 4U9E
| Entry DOI | 10.2210/pdb4u9e/pdb |
| Related | 4U9D |
| Descriptor | Soluble cytochrome b562, HEME C, CALCIUM ION, ... (5 entities in total) |
| Functional Keywords | designed enzyme, zn-coordinating protein, tetramer assembly, electron transport |
| Biological source | Escherichia coli |
| Total number of polymer chains | 1 |
| Total formula weight | 12654.81 |
| Authors | Tezcan, F.A.,Song, W.J. (deposition date: 2014-08-06, release date: 2015-01-21, Last modification date: 2024-10-23) |
| Primary citation | Song, W.J.,Tezcan, A.F. A designed supramolecular protein assembly with in vivo enzymatic activity Science, 346:1525-, 2014 Cited by PubMed Abstract: The generation of new enzymatic activities has mainly relied on repurposing the interiors of preexisting protein folds because of the challenge in designing functional, three-dimensional protein structures from first principles. Here we report an artificial metallo-β-lactamase, constructed via the self-assembly of a structurally and functionally unrelated, monomeric redox protein into a tetrameric assembly that possesses catalytic zinc sites in its interfaces. The designed metallo-β-lactamase is functional in the Escherichia coli periplasm and enables the bacteria to survive treatment with ampicillin. In vivo screening of libraries has yielded a variant that displays a catalytic proficiency [(k(cat)/K(m))/k(uncat)] for ampicillin hydrolysis of 2.3 × 10(6) and features the emergence of a highly mobile loop near the active site, a key component of natural β-lactamases to enable substrate interactions. PubMed: 25525249DOI: 10.1126/science.1259680 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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