1fgo

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[[Image:1fgo.jpg|left|200px]]
[[Image:1fgo.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 1fgo |SIZE=350|CAPTION= <scene name='initialview01'>1fgo</scene>, resolution 1.62&Aring;
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The line below this paragraph, containing "STRUCTURE_1fgo", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=FE:FE+(III)+ION'>FE</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/Lipoxygenase Lipoxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.11.12 1.13.11.12] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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|DOMAIN=
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{{STRUCTURE_1fgo| PDB=1fgo | SCENE= }}
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|RELATEDENTRY=[[1yge|1YGE]], [[1f8n|1F8N]], [[1fgm|1FGM]], [[1fgq|1FGQ]], [[1fgr|1FGR]], [[1fgt|1FGT]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fgo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fgo OCA], [http://www.ebi.ac.uk/pdbsum/1fgo PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1fgo RCSB]</span>
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}}
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'''LIPOXYGENASE-1 (SOYBEAN) AT 100K, Q495A MUTANT'''
'''LIPOXYGENASE-1 (SOYBEAN) AT 100K, Q495A MUTANT'''
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[[Category: Minor, W.]]
[[Category: Minor, W.]]
[[Category: Tomchick, D R.]]
[[Category: Tomchick, D R.]]
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[[Category: dioxygenase]]
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[[Category: Dioxygenase]]
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[[Category: fatty acid]]
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[[Category: Fatty acid]]
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[[Category: lipoxygenase]]
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[[Category: Lipoxygenase]]
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[[Category: metalloprotein]]
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[[Category: Metalloprotein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:18:19 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:22:32 2008''
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Revision as of 13:18, 2 May 2008

Image:1fgo.jpg

Template:STRUCTURE 1fgo

LIPOXYGENASE-1 (SOYBEAN) AT 100K, Q495A MUTANT


Overview

Lipoxygenases are an important class of non-heme iron enzymes that catalyze the hydroperoxidation of unsaturated fatty acids. The details of the enzymatic mechanism of lipoxygenases are still not well understood. This study utilizes a combination of kinetic and structural probes to relate the lipoxygenase mechanism of action with structural modifications of the iron's second coordination sphere. The second coordination sphere consists of Gln(495) and Gln(697), which form a hydrogen bond network between the substrate cavity and the first coordination sphere (Asn(694)). In this investigation, we compared the kinetic and structural properties of four mutants (Q495E, Q495A, Q697N, and Q697E) with those of wild-type soybean lipoxygenase-1 and determined that changes in the second coordination sphere affected the enzymatic activity by hydrogen bond rearrangement and substrate positioning through interaction with Gln(495). The nature of the C-H bond cleavage event remained unchanged, which demonstrates that the mutations have not affected the mechanism of hydrogen atom tunneling. The unusual and dramatic inverse solvent isotope effect (SIE) observed for the Q697E mutant indicated that an Fe(III)-OH(-) is the active site base. A new transition state model for hydrogen atom abstraction is proposed.

About this Structure

1FGO is a Single protein structure of sequence from Glycine max. Full crystallographic information is available from OCA.

Reference

Structural and functional characterization of second-coordination sphere mutants of soybean lipoxygenase-1., Tomchick DR, Phan P, Cymborowski M, Minor W, Holman TR, Biochemistry. 2001 Jun 26;40(25):7509-17. PMID:11412104 Page seeded by OCA on Fri May 2 16:18:19 2008

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