2fzv
From Proteopedia
(Difference between revisions)
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<StructureSection load='2fzv' size='340' side='right'caption='[[2fzv]], [[Resolution|resolution]] 1.70Å' scene=''> | <StructureSection load='2fzv' size='340' side='right'caption='[[2fzv]], [[Resolution|resolution]] 1.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2fzv]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Shigella_flexneri_2a_str. | + | <table><tr><td colspan='2'>[[2fzv]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Shigella_flexneri_2a_str._2457T Shigella flexneri 2a str. 2457T]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FZV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FZV FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7Å</td></tr> |
| - | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr> |
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2fzv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fzv OCA], [https://pdbe.org/2fzv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fzv RCSB], [https://www.ebi.ac.uk/pdbsum/2fzv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fzv ProSAT], [https://www.topsan.org/Proteins/MCSG/2fzv TOPSAN]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2fzv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fzv OCA], [https://pdbe.org/2fzv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fzv RCSB], [https://www.ebi.ac.uk/pdbsum/2fzv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fzv ProSAT], [https://www.topsan.org/Proteins/MCSG/2fzv TOPSAN]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/ARREH_SHIFL ARREH_SHIFL] Has NADPH-dependent FMN reductase activity and very low azoreductase activity. No activity with NADH.<ref>PMID:17962405</ref> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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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/main_output.php?pdb_ID=2fzv ConSurf]. | </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/main_output.php?pdb_ID=2fzv ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | The arsH gene or its homologs are a frequent part of the arsenic resistance system in bacteria and eukaryotes. Although a specific biological function of the gene product is unknown, the ArsH protein was annotated as a member of the NADPH-dependent FMN reductase family based on a conserved (T/S)XRXXSX(T/S) fingerprint motif common for FMN binding proteins. Presented here are the first crystal structure of an ArsH protein from Shigella flexneri refined at 1.7 A resolution and results of enzymatic activity assays that revealed a strong NADPH-dependent FMN reductase and low azoreductase activities. The ArsH apo protein has an alpha/beta/alpha-fold typical for FMN binding proteins. The asymmetric unit consists of four monomers, which form a tetramer. Buried surface analysis suggests that this tetramer is likely to be the relevant biological assembly. Dynamic light scattering experiments are consistent with this hypothesis and show that ArsH in solution at room temperature does exist predominantly in the tetrameric form. | ||
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| - | Crystal structure of an apo form of Shigella flexneri ArsH protein with an NADPH-dependent FMN reductase activity.,Vorontsov II, Minasov G, Brunzelle JS, Shuvalova L, Kiryukhina O, Collart FR, Anderson WF Protein Sci. 2007 Nov;16(11):2483-90. PMID:17962405<ref>PMID:17962405</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 2fzv" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Shigella flexneri 2a str. | + | [[Category: Shigella flexneri 2a str. 2457T]] |
| - | [[Category: Anderson | + | [[Category: Anderson WF]] |
| - | [[Category: Brunzelle | + | [[Category: Brunzelle JS]] |
| - | [[Category: Collart | + | [[Category: Collart FR]] |
| - | [[Category: Joachimiak | + | [[Category: Joachimiak A]] |
| - | + | [[Category: Minasov G]] | |
| - | [[Category: Minasov | + | [[Category: Shuvalova L]] |
| - | [[Category: Shuvalova | + | [[Category: Vorontsov II]] |
| - | [[Category: Vorontsov | + | |
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Current revision
Crystal Structure of an apo form of a Flavin-binding Protein from Shigella flexneri
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