1fgo

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{{Seed}}
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==LIPOXYGENASE-1 (SOYBEAN) AT 100K, Q495A MUTANT==
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[[Image:1fgo.png|left|200px]]
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<StructureSection load='1fgo' size='340' side='right' caption='[[1fgo]], [[Resolution|resolution]] 1.62&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1fgo]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Glycine_max Glycine max]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FGO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FGO FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene><br>
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<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1yge|1yge]], [[1f8n|1f8n]], [[1fgm|1fgm]], [[1fgq|1fgq]], [[1fgr|1fgr]], [[1fgt|1fgt]]</td></tr>
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<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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.rcsb.org/pdb/explore.do?structureId=1fgo RCSB], [http://www.ebi.ac.uk/pdbsum/1fgo PDBsum]</span></td></tr>
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<table>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fg/1fgo_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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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<ref>PMID:11412104</ref>
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The line below this paragraph, containing "STRUCTURE_1fgo", creates the "Structure Box" on the page.
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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or leave the SCENE parameter empty for the default display.
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-->
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{{STRUCTURE_1fgo| PDB=1fgo | SCENE= }}
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===LIPOXYGENASE-1 (SOYBEAN) AT 100K, Q495A MUTANT===
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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== References ==
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<!--
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<references/>
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The line below this paragraph, {{ABSTRACT_PUBMED_11412104}}, adds the Publication Abstract to the page
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__TOC__
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(as it appears on PubMed at http://www.pubmed.gov), where 11412104 is the PubMed ID number.
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</StructureSection>
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-->
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{{ABSTRACT_PUBMED_11412104}}
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==About this Structure==
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1FGO is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Glycine_max Glycine max]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FGO OCA].
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==Reference==
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<ref group="xtra">PMID:11412104</ref><references group="xtra"/>
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[[Category: Glycine max]]
[[Category: Glycine max]]
[[Category: Lipoxygenase]]
[[Category: Lipoxygenase]]
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[[Category: Lipoxygenase]]
[[Category: Lipoxygenase]]
[[Category: Metalloprotein]]
[[Category: Metalloprotein]]
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[[Category: Oxidoreductase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 21:50:00 2009''
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Revision as of 09:41, 28 September 2014

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

1fgo, resolution 1.62Å

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