3P7Y
Pentaerythritol tetranitrate reductase co-crystal structure with bound (E)-1-(2'-hydroxyphenyl)-2-nitroethene
Summary for 3P7Y
| Entry DOI | 10.2210/pdb3p7y/pdb |
| Related | 3P62 3P67 3P74 3P80 3P81 3P82 3P84 3P8I 3P8J |
| Descriptor | Pentaerythritol tetranitrate reductase, FLAVIN MONONUCLEOTIDE, 2-[(E)-2-nitroethenyl]phenol, ... (4 entities in total) |
| Functional Keywords | old yellow enzyme family, alpha, beta barrel, oxidoreductase |
| Biological source | Enterobacter cloacae |
| Total number of polymer chains | 1 |
| Total formula weight | 40156.69 |
| Authors | Toogood, H.S.,Scrutton, N.S. (deposition date: 2010-10-13, release date: 2011-03-02, Last modification date: 2023-09-06) |
| Primary citation | Toogood, H.S.,Fryszkowska, A.,Hulley, M.,Sakuma, M.,Mansell, D.,Stephens, G.M.,Gardiner, J.M.,Scrutton, N.S. A Site-Saturated Mutagenesis Study of Pentaerythritol Tetranitrate Reductase Reveals that Residues 181 and 184 Influence Ligand Binding, Stereochemistry and Reactivity. Chembiochem, 12:738-749, 2011 Cited by PubMed Abstract: We have conducted a site-specific saturation mutagenesis study of H181 and H184 of flavoprotein pentaerythritol tetranitrate reductase (PETN reductase) to probe the role of these residues in substrate binding and catalysis with a variety of α,β-unsaturated alkenes. Single mutations at these residues were sufficient to dramatically increase the enantiopurity of products formed by reduction of 2-phenyl-1-nitropropene. In addition, many mutants exhibited a switch in reactivity to predominantly catalyse nitro reduction, as opposed to CC reduction. These mutants showed an enhancement in a minor side reaction and formed 2-phenylpropanal oxime from 2-phenyl-1-nitropropene. The multiple binding conformations of hydroxy substituted nitro-olefins in PETN reductase were examined by using both structural and catalytic techniques. These compounds were found to bind in both active and inhibitory complexes; this highlights the plasticity of the active site and the ability of the H181/H184 couple to coordinate with multiple functional groups. These properties demonstrate the potential to use PETN reductase as a scaffold in the development of industrially useful biocatalysts. PubMed: 21374779DOI: 10.1002/cbic.201000662 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.2 Å) |
Structure validation
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