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==== | ==Aeronamide N-methyltransferase, AerE, bound to modified peptide substrate, AerA-DL,34== | ||
<StructureSection load='7rc6' size='340' side='right'caption='[[7rc6]]' scene=''> | <StructureSection load='7rc6' size='340' side='right'caption='[[7rc6]], [[Resolution|resolution]] 1.71Å' 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= OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol= FirstGlance]. <br> | <table><tr><td colspan='2'>[[7rc6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Microvirgula_aerodenitrificans_DSM_15089 Microvirgula aerodenitrificans DSM 15089]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7RC6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7RC6 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=7rc6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7rc6 OCA], [https://pdbe.org/7rc6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7rc6 RCSB], [https://www.ebi.ac.uk/pdbsum/7rc6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7rc6 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]] 1.71Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DAL:D-ALANINE'>DAL</scene>, <scene name='pdbligand=DLE:D-LEUCINE'>DLE</scene>, <scene name='pdbligand=DSG:D-ASPARAGINE'>DSG</scene>, <scene name='pdbligand=DTH:D-THREONINE'>DTH</scene>, <scene name='pdbligand=DVA:D-VALINE'>DVA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</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=7rc6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7rc6 OCA], [https://pdbe.org/7rc6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7rc6 RCSB], [https://www.ebi.ac.uk/pdbsum/7rc6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7rc6 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A2S0PEL5_9NEIS A0A2S0PEL5_9NEIS] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
SignificanceThe channel-forming proteusins are bacterial helical peptides that allow permeation of positively charged ions to influence membrane potential and cellular physiology. We biochemically characterize the effect of two critical posttranslational modifications on the secondary structure of the peptide substrate. We determine how a methyl group can be added to the side chains of D-Asn residues in a peptide substrate and show how flanking residues influence selectivity. These studies should foster the development of small-molecule peptide ion channels as therapeutics. | |||
Structure and mechanism for iterative amide N-methylation in the biosynthesis of channel-forming peptide cytotoxins.,Cogan DP, Bhushan A, Reyes R, Zhu L, Piel J, Nair SK Proc Natl Acad Sci U S A. 2022 Mar 29;119(13):e2116578119. doi:, 10.1073/pnas.2116578119. Epub 2022 Mar 22. PMID:35316135<ref>PMID:35316135</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7rc6" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Microvirgula aerodenitrificans DSM 15089]] | ||
[[Category: Cogan DP]] | |||
[[Category: Nair SK]] | |||
[[Category: Reyes R]] | |||
Latest revision as of 19:28, 18 October 2023
Aeronamide N-methyltransferase, AerE, bound to modified peptide substrate, AerA-DL,34Aeronamide N-methyltransferase, AerE, bound to modified peptide substrate, AerA-DL,34
Structural highlights
FunctionPublication Abstract from PubMedSignificanceThe channel-forming proteusins are bacterial helical peptides that allow permeation of positively charged ions to influence membrane potential and cellular physiology. We biochemically characterize the effect of two critical posttranslational modifications on the secondary structure of the peptide substrate. We determine how a methyl group can be added to the side chains of D-Asn residues in a peptide substrate and show how flanking residues influence selectivity. These studies should foster the development of small-molecule peptide ion channels as therapeutics. Structure and mechanism for iterative amide N-methylation in the biosynthesis of channel-forming peptide cytotoxins.,Cogan DP, Bhushan A, Reyes R, Zhu L, Piel J, Nair SK Proc Natl Acad Sci U S A. 2022 Mar 29;119(13):e2116578119. doi:, 10.1073/pnas.2116578119. Epub 2022 Mar 22. PMID:35316135[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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