7oey: Difference between revisions
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==Neisseria gonnorhoeae variant E93Q at 1.35 angstrom resolution== | ==Neisseria gonnorhoeae variant E93Q at 1.35 angstrom resolution== | ||
<StructureSection load='7oey' size='340' side='right'caption='[[7oey]]' scene=''> | <StructureSection load='7oey' size='340' side='right'caption='[[7oey]], [[Resolution|resolution]] 1.35Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7OEY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7OEY FirstGlance]. <br> | <table><tr><td colspan='2'>[[7oey]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Neisseria_gonorrhoeae_FA_1090 Neisseria gonorrhoeae FA 1090]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7OEY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7OEY FirstGlance]. <br> | ||
</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=7oey FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7oey OCA], [https://pdbe.org/7oey PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7oey RCSB], [https://www.ebi.ac.uk/pdbsum/7oey PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7oey ProSAT]</span></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]] 1.35Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SIN:SUCCINIC+ACID'>SIN</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=7oey FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7oey OCA], [https://pdbe.org/7oey PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7oey RCSB], [https://www.ebi.ac.uk/pdbsum/7oey PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7oey ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/TAL_NEIG1 TAL_NEIG1] Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway (By similarity). | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
We recently reported the discovery of a lysine-cysteine redox switch in proteins with a covalent nitrogen-oxygen-sulfur (NOS) bridge. Here, a systematic survey of the whole protein structure database discloses that NOS bridges are ubiquitous redox switches in proteins of all domains of life and are found in diverse structural motifs and chemical variants. In several instances, lysines are observed in simultaneous linkage with two cysteines, forming a sulfur-oxygen-nitrogen-oxygen-sulfur (SONOS) bridge with a trivalent nitrogen, which constitutes an unusual native branching cross-link. In many proteins, the NOS switch contains a functionally essential lysine with direct roles in enzyme catalysis or binding of substrates, DNA or effectors, linking lysine chemistry and redox biology as a regulatory principle. NOS/SONOS switches are frequently found in proteins from human and plant pathogens, including severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), and also in many human proteins with established roles in gene expression, redox signaling and homeostasis in physiological and pathophysiological conditions. | |||
Widespread occurrence of covalent lysine-cysteine redox switches in proteins.,Rabe von Pappenheim F, Wensien M, Ye J, Uranga J, Irisarri I, de Vries J, Funk LM, Mata RA, Tittmann K Nat Chem Biol. 2022 Feb 14. pii: 10.1038/s41589-021-00966-5. doi:, 10.1038/s41589-021-00966-5. PMID:35165445<ref>PMID:35165445</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7oey" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Transaldolase 3D structures|Transaldolase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Neisseria gonorrhoeae FA 1090]] | |||
[[Category: Rabe von Pappenheim F]] | [[Category: Rabe von Pappenheim F]] | ||
[[Category: Tittmann K]] | [[Category: Tittmann K]] | ||
[[Category: Wensien M]] | [[Category: Wensien M]] | ||