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.


1u5u

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1u5u" size="450" color="white" frame="true" align="right" spinBox="true" caption="1u5u, resolution 2.00&Aring;" /> '''The structure of an ...)
Current revision (08:44, 14 February 2024) (edit) (undo)
 
(14 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1u5u.gif|left|200px]]<br /><applet load="1u5u" size="450" color="white" frame="true" align="right" spinBox="true"
 
-
caption="1u5u, resolution 2.00&Aring;" />
 
-
'''The structure of an Allene Oxide Synthase reveals a novel use for a catalase fold'''<br />
 
-
==Overview==
+
==The structure of an Allene Oxide Synthase reveals a novel use for a catalase fold==
-
8R-Lipoxygenase and allene oxide synthase (AOS) are parts of a naturally, occurring fusion protein from the coral Plexaura homomalla. AOS catalyses, the production of an unstable epoxide (an allene oxide) from the fatty, acid hydroperoxide generated by the lipoxygenase activity. Here, we report, the structure of the AOS domain and its striking structural homology to, catalase. Whereas nominal sequence identity between the enzymes had been, previously described, the extent of structural homology observed was not, anticipated, given that this enzyme activity had been exclusively, associated with the P450 superfamily, and conservation of a catalase fold, without catalase activity is unprecedented. Whereas the heme environment, is largely conserved, the AOS heme is planar and the distal histidine is, flanked by two hydrogen-bonding residues. These critical differences, likely facilitate the switch from a catalatic activity to that of a fatty, acid hydroperoxidase.
+
<StructureSection load='1u5u' size='340' side='right'caption='[[1u5u]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
-
 
+
== Structural highlights ==
-
==About this Structure==
+
<table><tr><td colspan='2'>[[1u5u]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Plexaura_homomalla Plexaura homomalla]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U5U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1U5U FirstGlance]. <br>
-
1U5U is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Plexaura_homomalla Plexaura homomalla] with HEM as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Hydroperoxide_dehydratase Hydroperoxide dehydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.92 4.2.1.92] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1U5U OCA].
+
</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&#8491;</td></tr>
-
 
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>
-
==Reference==
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1u5u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u5u OCA], [https://pdbe.org/1u5u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1u5u RCSB], [https://www.ebi.ac.uk/pdbsum/1u5u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1u5u ProSAT]</span></td></tr>
-
The structure of coral allene oxide synthase reveals a catalase adapted for metabolism of a fatty acid hydroperoxide., Oldham ML, Brash AR, Newcomer ME, Proc Natl Acad Sci U S A. 2005 Jan 11;102(2):297-302. Epub 2004 Dec 29. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15625113 15625113]
+
</table>
-
[[Category: Hydroperoxide dehydratase]]
+
== Function ==
 +
[https://www.uniprot.org/uniprot/AOSL_PLEHO AOSL_PLEHO] Bifunctional enzyme which is responsible for allene oxide biosynthesis via a two-step reaction which involves conversion of arachidonic acid to a 8R-hydroperoxide intermediate followed by conversion of the hydroperoxide to allene oxide.<ref>PMID:9302294</ref> <ref>PMID:10559269</ref>
 +
== 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/u5/1u5u_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/main_output.php?pdb_ID=1u5u ConSurf].
 +
<div style="clear:both"></div>
 +
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
 +
[[Category: Large Structures]]
[[Category: Plexaura homomalla]]
[[Category: Plexaura homomalla]]
-
[[Category: Single protein]]
+
[[Category: Brash AR]]
-
[[Category: Brash, A.R.]]
+
[[Category: Newcomer ME]]
-
[[Category: Newcomer, M.E.]]
+
[[Category: Oldham ML]]
-
[[Category: Oldham, M.L.]]
+
-
[[Category: HEM]]
+
-
[[Category: allene oxide synthase]]
+
-
[[Category: catalase]]
+
-
[[Category: eicosanoid]]
+
-
[[Category: fusion protein]]
+
-
[[Category: heme]]
+
-
 
+
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 03:52:00 2007''
+

Current revision

The structure of an Allene Oxide Synthase reveals a novel use for a catalase fold

PDB ID 1u5u

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/1u5u"
Personal tools