2bmw

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[[Image:2bmw.png|left|200px]]
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==FERREDOXIN: NADP+REDUCTASE MUTANT WITH THR 155 REPLACED BY GLY, ALA 160 REPLACED BY THR, LEU 263 REPLACED BY PRO, ARG 264 REPLACED BY PRO AND GLY 265 REPLACED BY PRO (T155G-A160T-L263P-R264P-G265P)==
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<StructureSection load='2bmw' size='340' side='right' caption='[[2bmw]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2bmw]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Anabaena_sp. Anabaena sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BMW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2BMW FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br>
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<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1b2r|1b2r]], [[1bjk|1bjk]], [[1bqe|1bqe]], [[1e62|1e62]], [[1e63|1e63]], [[1e64|1e64]], [[1ewy|1ewy]], [[1gjr|1gjr]], [[1go2|1go2]], [[1gr1|1gr1]], [[1h42|1h42]], [[1h85|1h85]], [[1ogi|1ogi]], [[1ogj|1ogj]], [[1qgy|1qgy]], [[1qgz|1qgz]], [[1qh0|1qh0]], [[1que|1que]], [[1quf|1quf]], [[1w34|1w34]], [[1w35|1w35]], [[1w87|1w87]], [[2bsa|2bsa]]</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/Ferredoxin--NADP(+)_reductase Ferredoxin--NADP(+) reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.18.1.2 1.18.1.2] </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=2bmw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bmw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2bmw RCSB], [http://www.ebi.ac.uk/pdbsum/2bmw 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/bm/2bmw_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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Helicobacter pylori flavodoxin is the electronic acceptor of the pyruvate-oxidoreductase complex (POR) that catalyzes pyruvate oxidative decarboxilation. Inactivation of this metabolic route precludes bacterial survival. Because flavodoxin is not present in the human host, substances interfering electronic transport from POR might be well suited for eradication therapies against the bacterium. H. pylori flavodoxin presents a peculiar cofactor (FMN) binding site, compared to other known flavodoxins, where a conserved aromatic residue is replaced by alanine. A cavity thus appears under the cofactor that can be filled with small organic molecules. We have cloned H. pylori fldA gene, expressed the protein in Escherichia coli and characterized the purified flavodoxin. Thermal up-shift assays of flavodoxin with different concentrations of benzylamine, as well as fluorescence titration experiments indicate benzylamine binds in the pocket near the FMN binding site. It seems thus that low affinity inhibitors of H. pylori flavodoxin can be easily found that, after improvement, may give rise to leads.
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{{STRUCTURE_2bmw| PDB=2bmw | SCENE= }}
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Towards a new therapeutic target: Helicobacter pylori flavodoxin.,Cremades N, Bueno M, Toja M, Sancho J Biophys Chem. 2005 Apr 1;115(2-3):267-76. Epub 2005 Jan 7. PMID:15752617<ref>PMID:15752617</ref>
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===FERREDOXIN: NADP+REDUCTASE MUTANT WITH THR 155 REPLACED BY GLY, ALA 160 REPLACED BY THR, LEU 263 REPLACED BY PRO, ARG 264 REPLACED BY PRO AND GLY 265 REPLACED BY PRO (T155G-A160T-L263P-R264P-G265P)===
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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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{{ABSTRACT_PUBMED_15752617}}
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== References ==
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<references/>
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==About this Structure==
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__TOC__
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[[2bmw]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Anabaena_sp. Anabaena sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BMW OCA].
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</StructureSection>
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==Reference==
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<ref group="xtra">PMID:015752617</ref><ref group="xtra">PMID:019219975</ref><references group="xtra"/>
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[[Category: Anabaena sp.]]
[[Category: Anabaena sp.]]
[[Category: Gomez-Moreno, C.]]
[[Category: Gomez-Moreno, C.]]

Revision as of 02:24, 30 September 2014

FERREDOXIN: NADP+REDUCTASE MUTANT WITH THR 155 REPLACED BY GLY, ALA 160 REPLACED BY THR, LEU 263 REPLACED BY PRO, ARG 264 REPLACED BY PRO AND GLY 265 REPLACED BY PRO (T155G-A160T-L263P-R264P-G265P)

2bmw, resolution 1.50Å

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