3WFZ
Crystal structure of Galacto-N-Biose/Lacto-N-Biose I Phosphorylase C236Y Mutant
Summary for 3WFZ
| Entry DOI | 10.2210/pdb3wfz/pdb |
| Related | 2ZUU |
| Descriptor | Lacto-N-biose phosphorylase, 2-acetamido-2-deoxy-alpha-D-glucopyranose (3 entities in total) |
| Functional Keywords | beta-alpha-barrel, tim barrel, phosphorylase, transferase |
| Biological source | Bifidobacterium longum |
| Total number of polymer chains | 4 |
| Total formula weight | 343061.21 |
| Authors | Koyama, Y.,Hidaka, M.,Kawakami, M.,Nishimoto, M.,Kitaoka, M. (deposition date: 2013-07-25, release date: 2013-10-09, Last modification date: 2023-11-08) |
| Primary citation | Koyama, Y.,Hidaka, M.,Nishimoto, M.,Kitaoka, M. Directed evolution to enhance thermostability of galacto-N-biose/lacto-N-biose I phosphorylase. Protein Eng.Des.Sel., 26:755-761, 2013 Cited by PubMed Abstract: Galacto-N-biose/lacto-N-biose I phosphorylase (GLNBP) is the key enzyme in the enzymatic production of lacto-N-biose I. For the purpose of industrial use, we improved the thermostability of GLNBP by evolutionary engineering in which five substitutions in the amino acid sequence were selected from a random mutagenesis GLNBP library constructed using error-prone polymerase chain reaction. Among them, C236Y and D576V mutants showed considerably improved thermostability. Structural analysis of C236Y revealed that the hydroxyl group of Tyr236 forms a hydrogen bond with the carboxyl group of E319. The C236Y and D576V mutations together contributed to the thermostability. The C236Y/D576V mutant exhibited 20°C higher thermostability than the wild type. PubMed: 24065834DOI: 10.1093/protein/gzt049 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
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