2fnq
From Proteopedia
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| - | [[Image:2fnq.gif|left|200px]] | + | [[Image:2fnq.gif|left|200px]] |
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| - | '''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''' | + | {{Structure |
| + | |PDB= 2fnq |SIZE=350|CAPTION= <scene name='initialview01'>2fnq</scene>, resolution 3.200Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene> and <scene name='pdbligand=CA:CALCIUM ION'>CA</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] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''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''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2FNQ is a [ | + | 2FNQ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Plexaura_homomalla Plexaura homomalla]. This structure supersedes the now removed PDB entry 1ZQ4. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FNQ OCA]. |
==Reference== | ==Reference== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/16162493 16162493] |
[[Category: Arachidonate 8-lipoxygenase]] | [[Category: Arachidonate 8-lipoxygenase]] | ||
[[Category: Plexaura homomalla]] | [[Category: Plexaura homomalla]] | ||
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[[Category: fatty acid]] | [[Category: fatty acid]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:54:40 2008'' |
Revision as of 14:54, 20 March 2008
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| , resolution 3.200Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Activity: | Arachidonate 8-lipoxygenase, with EC number 1.13.11.40 | ||||||
| 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
Overview
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 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.
Reference
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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