23fq: Difference between revisions

Line 1:

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

~~The entry~~ 23fq is ~~ON HOLD~~ ~~until Paper Publication~~

==Dipeptide removal from MccJ25 yields a new lasso peptide delta-VG==

~~Authors~~:

== Structural highlights ==

<table><tr><td colspan='2'>[[23fq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=23FQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=23FQ FirstGlance]. <br>

~~Description~~:

</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, models</td></tr>

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

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=23fq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=23fq OCA], [https://pdbe.org/23fq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=23fq RCSB], [https://www.ebi.ac.uk/pdbsum/23fq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=23fq ProSAT]</span></td></tr>

</table>

== Function ==

[https://www.uniprot.org/uniprot/MCJA_ECOLX MCJA_ECOLX] Peptide antibiotic that functions through inhibition of the bacterial DNA-dependent RNA polymerase (RNAP). May inhibit transcription by binding in RNAP secondary channel and blocking nucleotide substrates access to the catalytic center. Exhibits potent bacteriocidal activity against a range of Enterobacteriaceae, including several pathogenic E.coli, Salmonella and Shigella strains. Also acts on the cytoplasmic membrane of Salmonella newport, producing alteration of membrane permeability and disruption of the subsequent gradient dissipation, which inhibits several processes essential for cell viability, such as oxygen consumption. Induces bacterial filamentation in susceptible cells in a non-SOS-dependent way, but this phenotype may result from impaired transcription of genes coding for cell division proteins.<ref>PMID:11731133</ref> <ref>PMID:11443089</ref> <ref>PMID:12401787</ref>

== References ==

__TOC__

</StructureSection>

[[Category: Escherichia coli]]

[[Category: Large Structures]]

[[Category: Chang C-F]]

[[Category: Chu C-H]]

[[Category: Huang Y-P]]

[[Category: Tsai C-Y]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 23fq is ON HOLD  until Paper Publication
+==Dipeptide removal from MccJ25 yields a new lasso peptide delta-VG==
+<StructureSection load='23fq' size='340' side='right'caption='[[23fq]]' scene=''>
-Authors:
+== Structural highlights ==
+<table><tr><td colspan='2'>[[23fq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=23FQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=23FQ FirstGlance]. <br>
-Description:
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR,  models</td></tr>
-[[Category: Unreleased Structures]]
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=23fq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=23fq OCA], [https://pdbe.org/23fq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=23fq RCSB], [https://www.ebi.ac.uk/pdbsum/23fq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=23fq ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/MCJA_ECOLX MCJA_ECOLX] Peptide antibiotic that functions through inhibition of the bacterial DNA-dependent RNA polymerase (RNAP). May inhibit transcription by binding in RNAP secondary channel and blocking nucleotide substrates access to the catalytic center. Exhibits potent bacteriocidal activity against a range of Enterobacteriaceae, including several pathogenic E.coli, Salmonella and Shigella strains. Also acts on the cytoplasmic membrane of Salmonella newport, producing alteration of membrane permeability and disruption of the subsequent gradient dissipation, which inhibits several processes essential for cell viability, such as oxygen consumption. Induces bacterial filamentation in susceptible cells in a non-SOS-dependent way, but this phenotype may result from impaired transcription of genes coding for cell division proteins.<ref>PMID:11731133</ref> <ref>PMID:11443089</ref> <ref>PMID:12401787</ref>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Escherichia coli]]
+[[Category: Large Structures]]
+[[Category: Chang C-F]]
+[[Category: Chu C-H]]
+[[Category: Huang Y-P]]
+[[Category: Tsai C-Y]]