2fnq: Difference between revisions
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|PDB= 2fnq |SIZE=350|CAPTION= <scene name='initialview01'>2fnq</scene>, resolution 3.200Å | |PDB= 2fnq |SIZE=350|CAPTION= <scene name='initialview01'>2fnq</scene>, resolution 3.200Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene> | ||
|ACTIVITY= [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] | |ACTIVITY= <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> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1u5u|1u5u]] | |||
|RESOURCES=<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.ebi.ac.uk/pdbsum/2fnq PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2fnq RCSB]</span> | |||
}} | }} | ||
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[[Category: Newcomer, M E.]] | [[Category: Newcomer, M E.]] | ||
[[Category: Oldham, M L.]] | [[Category: Oldham, M L.]] | ||
[[Category: beta-barrel]] | [[Category: beta-barrel]] | ||
[[Category: c2-like domain]] | [[Category: c2-like domain]] | ||
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[[Category: fatty acid]] | [[Category: fatty acid]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:05:22 2008'' |
Revision as of 03:05, 31 March 2008
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, resolution 3.200Å | |||||||
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Ligands: | , | ||||||
Activity: | Arachidonate 8-lipoxygenase, with EC number 1.13.11.40 | ||||||
Related: | 1u5u
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Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
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
OverviewOverview
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.
About this StructureAbout this Structure
2FNQ is a Single protein structure of sequence from Plexaura homomalla. This structure supersedes the now removed PDB entry 1ZQ4. Full crystallographic information is available from OCA.
ReferenceReference
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
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