5ui6: Difference between revisions

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Unreleased structure'''
-The entry 5ui6 is ON HOLD
+==Solution NMR Structure of Lasso Peptide Acinetodin==
+<StructureSection load='5ui6' size='340' side='right'caption='[[5ui6]]' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5ui6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Acinetobacter_gyllenbergii_CIP_110306_=_MTCC_11365 Acinetobacter gyllenbergii CIP 110306 = MTCC 11365]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UI6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5UI6 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=5ui6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ui6 OCA], [https://pdbe.org/5ui6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ui6 RCSB], [https://www.ebi.ac.uk/pdbsum/5ui6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ui6 ProSAT]</span></td></tr>
+</table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+We report the bioinformatic prediction and structural validation of two lasso peptides, acinetodin and klebsidin, encoded by the genomes of several human-associated strains of Acinetobacter and Klebsiella. Computation of the three-dimensional structures of these peptides using NMR NOESY constraints verifies that they contain a lasso motif. Despite the lack of sequence similarity to each other or to microcin J25, a prototypical lasso peptide and transcription inhibitor from Escherichia coli, acinetodin and klebsidin also inhibit transcript elongation by the E. coli RNA polymerase by binding to a common site. Yet, unlike microcin J25, acinetodin and klebsidin are unable to permeate wild type E. coli cells and inhibit their growth. We show that the E. coli cells become sensitive to klebsidin when expressing the outer membrane receptor FhuA homologue from Klebsiella pneumoniae. It thus appears that specificity to a common target, the RNA polymerase secondary channel, can be attained by a surprisingly diverse set of primary sequences folded into a common threaded-lasso fold. In contrast, transport into cells containing sensitive targets appears to be much more specific and must be the major determinant of the narrow range of bioactivity of known lasso peptides.
-Authors:
+Acinetodin and Klebsidin, RNA Polymerase Targeting Lasso Peptides Produced by Human Isolates of Acinetobacter gyllenbergii and Klebsiella pneumoniae.,Metelev M, Arseniev A, Bushin LB, Kuznedelov K, Artamonova TO, Kondratenko R, Khodorkovskii M, Seyedsayamdost MR, Severinov K ACS Chem Biol. 2017 Feb 3. doi: 10.1021/acschembio.6b01154. PMID:28106375<ref>PMID:28106375</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 5ui6" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Acinetobacter gyllenbergii CIP 110306 = MTCC 11365]]
+[[Category: Large Structures]]
+[[Category: Bushin LB]]
+[[Category: Metelev M]]
+[[Category: Severinov K]]
+[[Category: Seyedsayamdost MR]]