5lao: Difference between revisions

Line 1:

~~'''Unreleased structure'''~~

The ~~entry 5lao~~ is ~~ON HOLD~~

==S-nitrosylated 3D NMR structure of the cytoplasmic rhodanese domain of the inner membrane protein YgaP from Escherichia coli==

== Structural highlights ==

<table><tr><td colspan='2'>[[5lao]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LAO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5LAO FirstGlance]. <br>

</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=5lao FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lao OCA], [http://pdbe.org/5lao PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5lao RCSB], [http://www.ebi.ac.uk/pdbsum/5lao PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5lao ProSAT]</span></td></tr>

</table>

== 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.

~~Authors~~:

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>

~~Description~~:

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

[[Category: ~~Unreleased Structures~~]]

</div>

== References ==

__TOC__

</StructureSection>

[[Category: Choe, S]]

[[Category: Eichmann, C]]

[[Category: Guntert, P]]

[[Category: Kwiatkowski, W]]

[[Category: Lipton, S A]]

[[Category: Maslennikov, I]]

[[Category: Nakamura, T]]

[[Category: Riek, R]]

[[Category: Tzitzilonis, C]]

[[Category: Membrane protein]]

[[Category: Protein]]

[[Category: S-nitrosylated rhodanese domain of ygap]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 5lao is ON HOLD
+==S-nitrosylated 3D NMR structure of the cytoplasmic rhodanese domain of the inner membrane protein YgaP from Escherichia coli==
+<StructureSection load='5lao' size='340' side='right' caption='[[5lao]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5lao]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LAO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5LAO FirstGlance]. <br>
+</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=5lao FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lao OCA], [http://pdbe.org/5lao PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5lao RCSB], [http://www.ebi.ac.uk/pdbsum/5lao PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5lao 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.
-Authors:
+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>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 5lao" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Choe, S]]
+[[Category: Eichmann, C]]
+[[Category: Guntert, P]]
+[[Category: Kwiatkowski, W]]
+[[Category: Lipton, S A]]
+[[Category: Maslennikov, I]]
+[[Category: Nakamura, T]]
+[[Category: Riek, R]]
+[[Category: Tzitzilonis, C]]
+[[Category: Membrane protein]]
+[[Category: Protein]]
+[[Category: S-nitrosylated rhodanese domain of ygap]]