6ns6: Difference between revisions
m Protected "6ns6" [edit=sysop:move=sysop] |
No edit summary |
||
| (3 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
The | ==Crystal structure of fungal lipoxygenase from Fusarium graminearum. P21 crystal form.== | ||
<StructureSection load='6ns6' size='340' side='right'caption='[[6ns6]], [[Resolution|resolution]] 3.30Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6ns6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Fusarium_graminearum_PH-1 Fusarium graminearum PH-1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6NS6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6NS6 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.3Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6ns6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ns6 OCA], [https://pdbe.org/6ns6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ns6 RCSB], [https://www.ebi.ac.uk/pdbsum/6ns6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ns6 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/I1REW2_GIBZE I1REW2_GIBZE] | |||
<div style="background-color:#fffaf0;"> | |||
== 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<ref>PMID:30861228</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 6ns6" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
[[Category: | <references/> | ||
[[Category: | __TOC__ | ||
[[Category: | </StructureSection> | ||
[[Category: | [[Category: Fusarium graminearum PH-1]] | ||
[[Category: Large Structures]] | |||
[[Category: Bartlett SG]] | |||
[[Category: Boeglin WE]] | |||
[[Category: Brash AR]] | |||
[[Category: Neau DB]] | |||
[[Category: Newcomer ME]] | |||
[[Category: Pakhomova S]] | |||
Latest revision as of 09:58, 11 October 2023
Crystal structure of fungal lipoxygenase from Fusarium graminearum. P21 crystal form.Crystal structure of fungal lipoxygenase from Fusarium graminearum. P21 crystal form.
Structural highlights
FunctionPublication Abstract from PubMedThe 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||||||