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1u5u

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Revision as of 09:36, 29 September 2021

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

Structural highlights

1u5u is a 2 chain structure with sequence from Black sea rod. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Activity:	Hydroperoxide dehydratase, with EC number 4.2.1.92
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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.^[1] ^[2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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:15625113^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Koljak R, Boutaud O, Shieh BH, Samel N, Brash AR. Identification of a naturally occurring peroxidase-lipoxygenase fusion protein. Science. 1997 Sep 26;277(5334):1994-6. PMID:9302294
↑ Boutaud O, Brash AR. Purification and catalytic activities of the two domains of the allene oxide synthase-lipoxygenase fusion protein of the coral Plexaura homomalla. J Biol Chem. 1999 Nov 19;274(47):33764-70. PMID:10559269
↑ Oldham ML, Brash AR, Newcomer ME. The structure of coral allene oxide synthase reveals a catalase adapted for metabolism of a fatty acid hydroperoxide. Proc Natl Acad Sci U S A. 2005 Jan 11;102(2):297-302. Epub 2004 Dec 29. PMID:15625113

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1u5u"

@@ Line 3: / Line 3: @@
 <StructureSection load='1u5u' size='340' side='right'caption='[[1u5u]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1u5u]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Black_sea_rod Black sea rod]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1U5U FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1u5u]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Black_sea_rod Black sea rod]. 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>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>
+</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>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>
+<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Hydroperoxide_dehydratase Hydroperoxide dehydratase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.92 4.2.1.92] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1u5u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u5u OCA], [http://pdbe.org/1u5u PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1u5u RCSB], [http://www.ebi.ac.uk/pdbsum/1u5u PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1u5u 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=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>
 </table>
 == Function ==
-[[http://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>
+[[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]]

1u5u

From Proteopedia

Revision as of 09:36, 29 September 2021

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

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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