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==Refined 3D NMR structure of the cytoplasmic rhodanese domain of the inner membrane protein YgaP from Escherichia coli==
<StructureSection load='5lam' size='340' side='right'caption='[[5lam]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5lam]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LAM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LAM FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=5lam FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lam OCA], [https://pdbe.org/5lam PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5lam RCSB], [https://www.ebi.ac.uk/pdbsum/5lam PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5lam ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/YGAP_ECOLI YGAP_ECOLI] 
<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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5lam" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli K-12]]
[[Category: Large Structures]]
[[Category: Choe S]]
[[Category: Eichmann C]]
[[Category: Guntert P]]
[[Category: Kwiatkowski W]]
[[Category: Lipton SA]]
[[Category: Maslennikov I]]
[[Category: Nakamura T]]
[[Category: Riek R]]
[[Category: Tzitzilonis C]]