5hbo
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Native rhodanese domain of YgaP prepared without DDT is both S-nitrosylated and S-sulfhydrated== | |
| + | <StructureSection load='5hbo' size='340' side='right' caption='[[5hbo]], [[Resolution|resolution]] 1.66Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5hbo]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HBO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5HBO FirstGlance]. <br> | ||
| + | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSS:S-MERCAPTOCYSTEINE'>CSS</scene>, <scene name='pdbligand=SNC:S-NITROSO-CYSTEINE'>SNC</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5hbl|5hbl]]</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=5hbo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hbo OCA], [http://pdbe.org/5hbo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5hbo RCSB], [http://www.ebi.ac.uk/pdbsum/5hbo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5hbo ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | S-Nitrosylation is well established as an important post-translational regulator in protein function and signaling. However, relatively little is known about its structural and dynamical consequences. We have investigated the effects of S-nitrosylation on the rhodanese domain of the Escherichia coli integral membrane protein YgaP by NMR, X-ray crystallography, and mass spectrometry. The results show that the active cysteine in the rhodanese domain of YgaP is subjected to two competing modifications: S-nitrosylation and S-sulfhydration, which are naturally occurring in vivo. It has been observed that in addition to inhibition of the sulfur transfer activity, S-nitrosylation of the active site residue Cys63 causes an increase in slow motion and a displacement of helix 5 due to a weakening of the interaction between the active site and the helix dipole. These findings provide an example of how nitrosative stress can exert action at the atomic level. | ||
| - | + | S-Nitrosylation Induces Structural and Dynamical Changes in a Rhodanese Family Protein.,Eichmann C, Tzitzilonis C, Nakamura T, Kwiatkowski W, Maslennikov I, Choe S, Lipton SA, Riek R J Mol Biol. 2016 Jul 27. pii: S0022-2836(16)30255-8. doi:, 10.1016/j.jmb.2016.07.010. PMID:27473602<ref>PMID:27473602</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| + | <div class="pdbe-citations 5hbo" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Choe, S]] | [[Category: Choe, S]] | ||
| - | [[Category: Tzitzilonis, C]] | ||
| - | [[Category: Kwiatkowski, W]] | ||
| - | [[Category: Riek, R]] | ||
| - | [[Category: Lipton, S.A]] | ||
[[Category: Eichmann, C]] | [[Category: Eichmann, C]] | ||
| + | [[Category: Kwiatkowski, W]] | ||
| + | [[Category: Lipton, S A]] | ||
[[Category: Maslennikov, I]] | [[Category: Maslennikov, I]] | ||
[[Category: Nakamura, T]] | [[Category: Nakamura, T]] | ||
| + | [[Category: Riek, R]] | ||
| + | [[Category: Tzitzilonis, C]] | ||
| + | [[Category: S-nitrosylation]] | ||
| + | [[Category: S-sulfhydration. rhodanese]] | ||
| + | [[Category: Transferase]] | ||
Revision as of 16:03, 10 August 2016
Native rhodanese domain of YgaP prepared without DDT is both S-nitrosylated and S-sulfhydrated
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