7M0O
DGT-28 EPSPS
Summary for 7M0O
| Entry DOI | 10.2210/pdb7m0o/pdb |
| Descriptor | 3-phosphoshikimate 1-carboxyvinyltransferase, PHOSPHATE ION, POTASSIUM ION, ... (4 entities in total) |
| Functional Keywords | 5-enolpyruvylshikimate-3-phosphate synthase, epsps, biosynthetic protein, transferase |
| Biological source | Streptomyces sviceus |
| Total number of polymer chains | 1 |
| Total formula weight | 43561.20 |
| Authors | Chekan, J.R.,Nair, S.K. (deposition date: 2021-03-11, release date: 2021-04-14, Last modification date: 2023-10-18) |
| Primary citation | Griffin, S.L.,Chekan, J.R.,Lira, J.M.,Robinson, A.E.,Yerkes, C.N.,Siehl, D.L.,Wright, T.R.,Nair, S.K.,Cicchillo, R.M. Characterization of a Glyphosate-Tolerant Enzyme from Streptomyces svecius : A Distinct Class of 5-Enolpyruvylshikimate-3-phosphate Synthases. J.Agric.Food Chem., 69:5096-5104, 2021 Cited by PubMed Abstract: Natural and modified versions of the 5-enolpyruvylshikimate-3-phosphate synthase () gene have been used to confer tolerance to the broad-spectrum herbicide glyphosate in a variety of commercial crops. The most widely utilized trait was obtained from the strain CP4 and has been commercialized in several glyphosate-tolerant crops. The EPSPS gene products are enzymes that have been divided into three classes based on sequence similarity, sensitivity to glyphosate, and steady-state catalytic parameters. Herein, we describe the informatics-guided identification and biochemical and structural characterization of a novel EPSPS from (DGT-28 EPSPS). The data suggest DGT-28 EPSPS and other closely related homologues exemplify a distinct new class (Class IV) of EPSPS enzymes that display intrinsic tolerance to high concentrations of glyphosate ( ≥ 5000 μM). We further demonstrate that , when transformed into stable plants, provides robust (≥4× field rates) vegetative/reproductive herbicide tolerance and has utility in weed-control systems comparable to that of commercialized events. PubMed: 33826316DOI: 10.1021/acs.jafc.1c00439 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.62 Å) |
Structure validation
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