3vf1: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
← Older edit
No edit summary
No edit summary
 
Line 4: Line 4:
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3vf1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Gersemia_fruticosa Gersemia fruticosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VF1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VF1 FirstGlance]. <br>
<table><tr><td colspan='2'>[[3vf1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Gersemia_fruticosa Gersemia fruticosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VF1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VF1 FirstGlance]. <br>
</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>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=FRU:FRUCTOSE'>FRU</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.473&#8491;</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>, <scene name='pdbligand=FRU:FRUCTOSE'>FRU</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=PRD_900003:sucrose'>PRD_900003</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=3vf1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vf1 OCA], [https://pdbe.org/3vf1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vf1 RCSB], [https://www.ebi.ac.uk/pdbsum/3vf1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vf1 ProSAT]</span></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=3vf1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vf1 OCA], [https://pdbe.org/3vf1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vf1 RCSB], [https://www.ebi.ac.uk/pdbsum/3vf1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vf1 ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[https://www.uniprot.org/uniprot/Q2N410_9CNID Q2N410_9CNID]
Lipoxygenases (LOXs) are a key part of several signaling pathways that lead to inflammation and cancer. Yet, the mechanisms of substrate binding and allosteric regulation by the various LOX isoforms remain speculative. Here we report the 2.47 A resolution crystal structure of the arachidonate 11R-LOX from Gersemia fruticosa which sheds new light on the mechanism of LOX catalysis. Our crystallographic and mutational studies suggest that the aliphatic tail of the fatty acid is bound in a hydrophobic pocket with two potential entrances. We speculate that LOXs share a common T-shaped substrate channel architecture that gives rise to the varying positional specificities. A general allosteric mechanism is proposed for transmitting the activity-inducing effect of calcium binding from the membrane-targeting PLAT (polycystin-1/lipoxygenase/alpha-toxin) domain to the active site via a conserved pi-cation bridge.
 
Structure of a calcium-dependent 11R-lipoxygenase suggests a mechanism for Ca2+-regulation.,Eek P, Jarving R, Jarving I, Gilbert NC, Newcomer ME, Samel N J Biol Chem. 2012 May 9. PMID:22573333<ref>PMID:22573333</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3vf1" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Gersemia fruticosa]]
[[Category: Gersemia fruticosa]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Eek, P]]
[[Category: Eek P]]
[[Category: Gilbert, N C]]
[[Category: Gilbert NC]]
[[Category: Jarving, I]]
[[Category: Jarving I]]
[[Category: Jarving, R]]
[[Category: Jarving R]]
[[Category: Newcomer, M E]]
[[Category: Newcomer ME]]
[[Category: Samel, N]]
[[Category: Samel N]]
[[Category: Beta sandwich]]
[[Category: C2-like domain]]
[[Category: Conformational change]]
[[Category: Dioxygenase]]
[[Category: Lox]]
[[Category: Non-heme iron]]
[[Category: Oxidoreductase]]
[[Category: Plat]]

Latest revision as of 13:35, 1 March 2024

Structure of a calcium-dependent 11R-lipoxygenase suggests a mechanism for Ca-regulationStructure of a calcium-dependent 11R-lipoxygenase suggests a mechanism for Ca-regulation

Structural highlights

3vf1 is a 2 chain structure with sequence from Gersemia fruticosa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.473Å
Ligands:, , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q2N410_9CNID

3vf1, resolution 2.47Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
Retrieved from "https://proteopedia.openfox.io/wiki/index.php?title=3vf1&oldid=4072737"