This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


2fnq

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
m (Protected "2fnq" [edit=sysop:move=sysop])
Line 1: Line 1:
-
[[Image:2fnq.png|left|200px]]
+
==Insights from the X-ray crystal structure of coral 8R-lipoxygenase: calcium activation via A C2-like domain and a structural basis of product chirality==
 +
<StructureSection load='2fnq' size='340' side='right' caption='[[2fnq]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[2fnq]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Plexaura_homomalla Plexaura homomalla]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1zq4 1zq4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FNQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2FNQ FirstGlance]. <br>
 +
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene><br>
 +
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1u5u|1u5u]]</td></tr>
 +
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Arachidonate_8-lipoxygenase Arachidonate 8-lipoxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.11.40 1.13.11.40] </span></td></tr>
 +
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2fnq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fnq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2fnq RCSB], [http://www.ebi.ac.uk/pdbsum/2fnq PDBsum]</span></td></tr>
 +
<table>
 +
== Evolutionary Conservation ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fn/2fnq_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Lipoxygenases (LOXs) catalyze the regio- and stereospecific dioxygenation of polyunsaturated membrane-embedded fatty acids. We report here the 3.2 A resolution structure of 8R-LOX from the Caribbean sea whip coral Plexaura homomalla, a LOX isozyme with calcium dependence and the uncommon R chiral stereospecificity. Structural and spectroscopic analyses demonstrated calcium binding in a C2-like membrane-binding domain, illuminating the function of similar amino acids in calcium-activated mammalian 5-LOX, the key enzyme in the pathway to the pro-inflammatory leukotrienes. Mutation of Ca(2+)-ligating amino acids in 8R-LOX resulted not only in a diminished capacity to bind membranes, as monitored by fluorescence resonance energy transfer, but also in an associated loss of Ca(2+)-regulated enzyme activity. Moreover, a structural basis for R chiral specificity is also revealed; creation of a small oxygen pocket next to Gly(428) (Ala in all S-LOX isozymes) promoted C-8 oxygenation with R chirality on the activated fatty acid substrate.
-
{{STRUCTURE_2fnq| PDB=2fnq | SCENE= }}
+
Insights from the X-ray crystal structure of coral 8R-lipoxygenase: calcium activation via a C2-like domain and a structural basis of product chirality.,Oldham ML, Brash AR, Newcomer ME J Biol Chem. 2005 Nov 25;280(47):39545-52. Epub 2005 Sep 14. PMID:16162493<ref>PMID:16162493</ref>
-
===Insights from the X-ray crystal structure of coral 8R-lipoxygenase: calcium activation via A C2-like domain and a structural basis of product chirality===
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
 
+
</div>
-
{{ABSTRACT_PUBMED_16162493}}
+
== References ==
-
 
+
<references/>
-
==About this Structure==
+
__TOC__
-
[[2fnq]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Plexaura_homomalla Plexaura homomalla]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1zq4 1zq4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FNQ OCA].
+
</StructureSection>
-
 
+
-
==Reference==
+
-
<ref group="xtra">PMID:016162493</ref><references group="xtra"/>
+
[[Category: Arachidonate 8-lipoxygenase]]
[[Category: Arachidonate 8-lipoxygenase]]
[[Category: Plexaura homomalla]]
[[Category: Plexaura homomalla]]

Revision as of 10:12, 30 September 2014

Insights from the X-ray crystal structure of coral 8R-lipoxygenase: calcium activation via A C2-like domain and a structural basis of product chirality

2fnq, resolution 3.20Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2fnq"
Views
Personal tools
Navigation
Toolbox