5hbl: Difference between revisions
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New page: '''Unreleased structure''' The entry 5hbl is ON HOLD Authors: Cedric Eichmann, Christos Tzitzilonis, Tomohiro Nakamura, Witek Kwiatkowski, Innokentiy Maslennikov, Senyon Choe, Stuart A.... |
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The | ==Native rhodanese domain of YgaP prepared with 1mM DDT is S-nitrosylated== | ||
<StructureSection load='5hbl' size='340' side='right'caption='[[5hbl]], [[Resolution|resolution]] 1.62Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5hbl]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HBL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5HBL FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.617Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SNC:S-NITROSO-CYSTEINE'>SNC</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=5hbl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hbl OCA], [https://pdbe.org/5hbl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5hbl RCSB], [https://www.ebi.ac.uk/pdbsum/5hbl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5hbl 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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 5hbl" style="background-color:#fffaf0;"></div> | ||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Escherichia coli]] | |||
[[Category: Large Structures]] | |||
[[Category: Choe S]] | |||
[[Category: Eichmann C]] | |||
[[Category: Kwiatkowski W]] | |||
[[Category: Lipton SA]] | |||
[[Category: Maslennikov I]] | |||
[[Category: Nakamura T]] | |||
[[Category: Riek R]] | |||
[[Category: Tzitzilonis C]] | |||
Latest revision as of 07:29, 9 August 2023
Native rhodanese domain of YgaP prepared with 1mM DDT is S-nitrosylated
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