6esk: Difference between revisions
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==Structure of the apo form of AioX from Rhizobium sp. str. NT-26== | |||
<StructureSection load='6esk' size='340' side='right' caption='[[6esk]], [[Resolution|resolution]] 1.75Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6esk]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ESK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6ESK FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></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=6esk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6esk OCA], [http://pdbe.org/6esk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6esk RCSB], [http://www.ebi.ac.uk/pdbsum/6esk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6esk ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Arsenic contamination of drinking water affects more than 140 million people worldwide. While toxic to humans, inorganic forms of arsenic (arsenite and arsenate), can be used as energy sources for microbial respiration. AioX and its orthologues (ArxX and ArrX) represent the first members of a new sub-family of periplasmic-binding proteins that serve as the first component of a signal transduction system, that's role is to positively regulate expression of arsenic metabolism enzymes. As determined by X-ray crystallography for AioX, arsenite binding only requires subtle conformational changes in protein structure, providing insights into protein-ligand interactions. The binding pocket of all orthologues is conserved but this alone is not sufficient for oxyanion selectivity, with proteins selectively binding either arsenite or arsenate. Phylogenetic evidence, clearly demonstrates that the regulatory proteins evolved together early in prokaryotic evolution and had a separate origin from the metabolic enzymes whose expression they regulate. | |||
A new family of periplasmic-binding proteins that sense arsenic oxyanions.,Badilla C, Osborne TH, Cole A, Watson C, Djordjevic S, Santini JM Sci Rep. 2018 Apr 19;8(1):6282. doi: 10.1038/s41598-018-24591-w. PMID:29674678<ref>PMID:29674678</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6esk" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Badilla, C]] | [[Category: Badilla, C]] | ||
[[Category: Cole, A]] | [[Category: Cole, A]] | ||
[[Category: Djordjevic, S]] | |||
[[Category: Santini, J]] | [[Category: Santini, J]] | ||
[[Category: Arsenic]] | |||
[[Category: Arsenite-binding]] | |||
[[Category: Periplasmic-binding protein]] | |||
[[Category: Rhizobium nt-26]] | |||
[[Category: Signaling protein]] | |||
Revision as of 11:03, 17 October 2018
Structure of the apo form of AioX from Rhizobium sp. str. NT-26Structure of the apo form of AioX from Rhizobium sp. str. NT-26
Structural highlights
Publication Abstract from PubMedArsenic contamination of drinking water affects more than 140 million people worldwide. While toxic to humans, inorganic forms of arsenic (arsenite and arsenate), can be used as energy sources for microbial respiration. AioX and its orthologues (ArxX and ArrX) represent the first members of a new sub-family of periplasmic-binding proteins that serve as the first component of a signal transduction system, that's role is to positively regulate expression of arsenic metabolism enzymes. As determined by X-ray crystallography for AioX, arsenite binding only requires subtle conformational changes in protein structure, providing insights into protein-ligand interactions. The binding pocket of all orthologues is conserved but this alone is not sufficient for oxyanion selectivity, with proteins selectively binding either arsenite or arsenate. Phylogenetic evidence, clearly demonstrates that the regulatory proteins evolved together early in prokaryotic evolution and had a separate origin from the metabolic enzymes whose expression they regulate. A new family of periplasmic-binding proteins that sense arsenic oxyanions.,Badilla C, Osborne TH, Cole A, Watson C, Djordjevic S, Santini JM Sci Rep. 2018 Apr 19;8(1):6282. doi: 10.1038/s41598-018-24591-w. PMID:29674678[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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