6ns3

Crystal structure of fungal lipoxygenase from Fusarium graminearum. I222 crystal form.

spinqualitylabelsall models 6ns3, resolution 2.84Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6ns3 is a 1 chain structure with sequence from Fusarium graminearum PH-1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.84Å Ligands: FE2 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function I1REW2_GIBZE Publication Abstract from PubMed The regio- and stereo- specific oxygenation of polyunsaturated fatty acids (PUFA) 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(2+) 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(2+) coordination sphere. This article is protected by copyright. All rights reserved. An ensemble of lipoxygenase structures reveals novel conformations of the Fe coordination sphere.,Pakhomova S, Boeglin WE, Neau DB, Bartlett SG, Brash AR, Newcomer ME Protein Sci. 2019 Mar 12. doi: 10.1002/pro.3602. PMID:30861228 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA