|
|
| Line 3: |
Line 3: |
| | <StructureSection load='5hbq' size='340' side='right'caption='[[5hbq]], [[Resolution|resolution]] 1.66Å' scene=''> | | <StructureSection load='5hbq' size='340' side='right'caption='[[5hbq]], [[Resolution|resolution]] 1.66Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5hbq]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HBQ OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5HBQ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5hbq]] 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=5HBQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5HBQ FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.66Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5hbl|5hbl]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ygaP, b2668, JW2643 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</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=5hbq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hbq OCA], [https://pdbe.org/5hbq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5hbq RCSB], [https://www.ebi.ac.uk/pdbsum/5hbq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5hbq ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5hbq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hbq OCA], [http://pdbe.org/5hbq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5hbq RCSB], [http://www.ebi.ac.uk/pdbsum/5hbq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5hbq ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/YGAP_ECOLI YGAP_ECOLI] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 22: |
Line 23: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus coli migula 1895]] | + | [[Category: Escherichia coli]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Choe, S]] | + | [[Category: Choe S]] |
| - | [[Category: Eichmann, C]] | + | [[Category: Eichmann C]] |
| - | [[Category: Kwiatkowski, W]] | + | [[Category: Kwiatkowski W]] |
| - | [[Category: Lipton, S A]] | + | [[Category: Lipton SA]] |
| - | [[Category: Maslennikov, I]] | + | [[Category: Maslennikov I]] |
| - | [[Category: Nakamura, T]] | + | [[Category: Nakamura T]] |
| - | [[Category: Riek, R]] | + | [[Category: Riek R]] |
| - | [[Category: Tzitzilonis, C]] | + | [[Category: Tzitzilonis C]] |
| - | [[Category: Rhodanese]]
| + | |
| - | [[Category: S-nitrosylation]]
| + | |
| - | [[Category: S-sulfhydration]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
YGAP_ECOLI
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Eichmann C, Tzitzilonis C, Nakamura T, Kwiatkowski W, Maslennikov I, Choe S, Lipton SA, Riek R. S-Nitrosylation Induces Structural and Dynamical Changes in a Rhodanese Family Protein. J Mol Biol. 2016 Jul 27. pii: S0022-2836(16)30255-8. doi:, 10.1016/j.jmb.2016.07.010. PMID:27473602 doi:http://dx.doi.org/10.1016/j.jmb.2016.07.010
|
