4oi3: Difference between revisions
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''' | ==Crystal structure analysis of SCO4226 from Streptomyces coelicolor A3(2)== | ||
<StructureSection load='4oi3' size='340' side='right' caption='[[4oi3]], [[Resolution|resolution]] 1.30Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4oi3]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OI3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4OI3 FirstGlance]. <br> | |||
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4oi6|4oi6]]</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4oi3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4oi3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4oi3 RCSB], [http://www.ebi.ac.uk/pdbsum/4oi3 PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The open reading frame SCO4226 of Streptomyces coelicolor A3(2) encodes an 82-residue hypothetical protein. Biochemical assays revealed that each SCO4226 dimer binds four nickel ions. To decipher the molecular function, we solved the crystal structures of SCO4226 in both apo- and nickel-bound (Ni-SCO4226) forms at 1.30 and 2.04 A resolution, respectively. Each subunit of SCO4226 dimer adopts a canonical ferredoxin-like fold with five beta-strands flanked by two alpha-helices. In the structure of Ni-SCO4226, four nickel ions are coordinated at the surface of the dimer. Further biochemical assays suggested that the binding of Ni2+ triggers the self-aggregation of SCO4226 in vitro. In addition, RT-qPCR assays demonstrated that the expression of SCO4226 gene in S. coelicolor is specifically up-regulated by the addition of Ni2+, but not other divalent ions such as Cu2+, Mn2+ or Co2+. All these results suggested that SCO4226 acts as a nickel binding protein, probably required for nickel sequestration and/or detoxification. | |||
Streptomyces coelicolor SCO4226 Is a Nickel Binding Protein.,Lu M, Jiang YL, Wang S, Jin H, Zhang RG, Virolle MJ, Chen Y, Zhou CZ PLoS One. 2014 Oct 6;9(10):e109660. doi: 10.1371/journal.pone.0109660., eCollection 2014. PMID:25285530<ref>PMID:25285530</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Chen, Y.]] | |||
[[Category: Cheng, W.]] | |||
[[Category: Jiang, Y L.]] | |||
[[Category: Lu, M.]] | |||
[[Category: Virolle, M J.]] | |||
[[Category: Wang, S.]] | |||
[[Category: Zhang, R G.]] | |||
[[Category: Zhou, C Z.]] | |||
[[Category: A nickel responsive protein]] | |||
[[Category: Ferredoxin-like fold]] | |||
[[Category: Metal binding protein]] | |||
[[Category: Nickel binding]] | |||
[[Category: Nickel responsive protein]] | |||
[[Category: Structural genomic]] | |||
Revision as of 08:43, 22 October 2014
Crystal structure analysis of SCO4226 from Streptomyces coelicolor A3(2)
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