6NS5
Crystal structure of fungal lipoxygenase from Fusarium graminearum. Second C2 crystal form.
Summary for 6NS5
| Entry DOI | 10.2210/pdb6ns5/pdb |
| Related | 6NS2 6NS3 6NS4 6NS6 |
| Descriptor | lipoxygenase, FE (II) ION (3 entities in total) |
| Functional Keywords | lipoxygenase, fungus, fe coordination, oxidoreductase |
| Biological source | Gibberella zeae (strain PH-1 / ATCC MYA-4620 / FGSC 9075 / NRRL 31084) (Wheat head blight fungus) |
| Total number of polymer chains | 2 |
| Total formula weight | 172925.22 |
| Authors | Pakhomova, S.,Boeglin, W.E.,Neau, D.B.,Bartlett, S.G.,Brash, A.R.,Newcomer, M.E. (deposition date: 2019-01-24, release date: 2019-03-27, Last modification date: 2023-10-11) |
| Primary citation | Pakhomova, S.,Boeglin, W.E.,Neau, D.B.,Bartlett, S.G.,Brash, A.R.,Newcomer, M.E. An ensemble of lipoxygenase structures reveals novel conformations of the Fe coordination sphere. Protein Sci., 28:920-927, 2019 Cited by PubMed Abstract: The regio- and stereo-specific oxygenation of polyunsaturated fatty acids is catalyzed by lipoxygenases (LOX); both Fe and Mn forms of the enzyme have been described. Structural elements of the Fe and Mn coordination spheres and the helical catalytic domain in which the metal center resides are highly conserved. However, animal, plant, and microbial LOX each have distinct features. We report five crystal structures of a LOX from the fungal plant pathogen Fusarium graminearum. This LOX displays a novel amino terminal extension that provides a wrapping domain for dimerization. Moreover, this extension appears to interfere with the iron coordination sphere, as the typical LOX configuration is not observed at the catalytic metal when the enzyme is dimeric. Instead novel tetra-, penta-, and hexa-coordinate Fe ligations are apparent. In contrast, a monomeric structure indicates that with repositioning of the amino terminal segment, the enzyme can assume a productive conformation with the canonical Fe coordination sphere. PubMed: 30861228DOI: 10.1002/pro.3602 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.79 Å) |
Structure validation
Download full validation report
