1u5u

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[[Image:1u5u.gif|left|200px]]
[[Image:1u5u.gif|left|200px]]
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{{Structure
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|PDB= 1u5u |SIZE=350|CAPTION= <scene name='initialview01'>1u5u</scene>, resolution 2.00&Aring;
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The line below this paragraph, containing "STRUCTURE_1u5u", creates the "Structure Box" on the page.
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|SITE=
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|LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <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>
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{{STRUCTURE_1u5u| PDB=1u5u | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<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://www.ebi.ac.uk/pdbsum/1u5u PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1u5u RCSB]</span>
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'''The structure of an Allene Oxide Synthase reveals a novel use for a catalase fold'''
'''The structure of an Allene Oxide Synthase reveals a novel use for a catalase fold'''
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[[Category: Newcomer, M E.]]
[[Category: Newcomer, M E.]]
[[Category: Oldham, M L.]]
[[Category: Oldham, M L.]]
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[[Category: allene oxide synthase]]
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[[Category: Allene oxide synthase]]
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[[Category: catalase]]
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[[Category: Catalase]]
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[[Category: eicosanoid]]
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[[Category: Eicosanoid]]
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[[Category: fusion protein]]
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[[Category: Fusion protein]]
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[[Category: heme]]
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[[Category: Heme]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 10:47:33 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:05:52 2008''
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Revision as of 07:47, 3 May 2008

Template:STRUCTURE 1u5u

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


Overview

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.

About this Structure

1U5U is a Single protein structure of sequence from Plexaura homomalla. Full crystallographic information is available from OCA.

Reference

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 Page seeded by OCA on Sat May 3 10:47:33 2008

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