7z6a: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older edit
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
No edit summary
 
Line 8: Line 8:
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7z6a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7z6a OCA], [https://pdbe.org/7z6a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7z6a RCSB], [https://www.ebi.ac.uk/pdbsum/7z6a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7z6a ProSAT]</span></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=7z6a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7z6a OCA], [https://pdbe.org/7z6a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7z6a RCSB], [https://www.ebi.ac.uk/pdbsum/7z6a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7z6a ProSAT]</span></td></tr>
</table>
</table>
== Function ==
<div style="background-color:#fffaf0;">
[https://www.uniprot.org/uniprot/FEMX_WEIVI FEMX_WEIVI] Involved in the synthesis of the bacterial cell wall. Catalyzes the addition of alanine into the interchain peptide bridge of peptidoglycan precursor using aminoacyl-tRNA(Ala) as amino acid donor. This alanine is added to the epsilon-amino group of the L-lysine of the peptidoglycan UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-L-lysyl-D-alanyl-D-alanine, in a ribosome-independent mechanism (PubMed:11083873, PubMed:4248527, PubMed:12679335, PubMed:15901708, PubMed:23744707). Specific for UDP-N-acetyl-muramoyl-pentapeptide. Has no activity toward UDP-N-acetyl-muramoyl-tetrapeptide or UDP-N-acetyl-muramoyl-tripeptide (PubMed:15901708). Also acts on L-seryl-tRNA(Ser) (PubMed:4248527).<ref>PMID:11083873</ref> <ref>PMID:12679335</ref> <ref>PMID:15901708</ref> <ref>PMID:23744707</ref> <ref>PMID:4248527</ref>  
== Publication Abstract from PubMed ==
Xenobiotic nucleic acids (XNAs) offer tremendous potential for synthetic biology, biotechnology, and molecular medicine but their ability to mimic nucleic acids still needs to be explored. Here, to study the ability of XNA oligonucleotides to mimic tRNA, we synthesized three L-Ala-tXNAs analogs. These molecules were used in a non-ribosomal peptide synthesis involving a bacterial Fem transferase. We compared the ability of this enzyme to use amino-acyl tXNAs containing 1',5'-anhydrohexitol (HNA), 2'-fluoro ribose (2'F-RNA) and 2'-fluoro arabinose. L-Ala-tXNA containing HNA or 2'F-RNA were substrates of the Fem enzyme. The synthesis of peptidyl-XNA and the resolution of their structures in complex with the enzyme show the impact of the XNA on protein binding. For the first time we describe functional tXNA in an in vitro assay. These results invite to test tXNA also as substitute for tRNA in translation.
 
Amino-acyl tXNA as inhibitors or amino acid donors in peptide synthesis.,Rietmeyer L, Li De La Sierra-Gallay I, Schepers G, Dorchene D, Iannazzo L, Patin D, Touze T, van Tilbeurgh H, Herdewijn P, Etheve-Quelquejeu M, Fonvielle M Nucleic Acids Res. 2022 Nov 11;50(20):11415-11425. doi: 10.1093/nar/gkac1023. PMID:36350642<ref>PMID:36350642</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7z6a" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
Retrieved from "https://proteopedia.org/7z6a"