8p5o: Difference between revisions

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'''Unreleased structure'''


The entry 8p5o is ON HOLD  until Paper Publication
==Proline activating adenylation domain of gramicidin S synthetase 2 - GrsB1-Acore==
<StructureSection load='8p5o' size='340' side='right'caption='[[8p5o]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8p5o]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Aneurinibacillus_migulanus Aneurinibacillus migulanus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8P5O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8P5O FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</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=8p5o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8p5o OCA], [https://pdbe.org/8p5o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8p5o RCSB], [https://www.ebi.ac.uk/pdbsum/8p5o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8p5o ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/GRSB_ANEMI GRSB_ANEMI] This protein is a multifunctional enzyme, able to activate and polymerize the amino acids Pro, Val, Orn and Leu. Activation sites for these AA consist of individual domains.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Engineering of biosynthetic enzymes is increasingly employed to synthesize structural analogues of antibiotics. Of special interest are non-ribosomal peptide synthetases (NRPSs) responsible for production of important antimicrobial peptides. Here, directed evolution of an adenylation domain of a Pro-specific NRPS module completely switched substrate specificity to the non-standard amino acid piperazic acid (Piz) bearing a labile N-N bond. This success was achieved by UPLC-MS/MS based screening of small, rationally designed mutant libraries and can presumably be replicated with a larger number of substrates and NRPS modules. The evolved NRPS produces a Piz-derived gramicidin S analogue. Thus, we give new impetus to the too-early dismissed idea that widely accessible low-throughput methods can switch the specificity of NRPSs in a biosynthetically useful fashion.


Authors: Stephan, P., Basquin, J., Caputi, L., O''Connor, S.E., Kries, H.
Directed Evolution of Piperazic Acid Incorporation by a Nonribosomal Peptide Synthetase.,Stephan P, Langley C, Winkler D, Basquin J, Caputi L, O'Connor SE, Kries H Angew Chem Int Ed Engl. 2023 Jun 16:e202304843. doi: 10.1002/anie.202304843. PMID:37326625<ref>PMID:37326625</ref>


Description: Proline activating adenylation domain of gramicidin S synthetase 2 -GrsB1-Acore
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Stephan, P]]
<div class="pdbe-citations 8p5o" style="background-color:#fffaf0;"></div>
[[Category: Caputi, L]]
== References ==
[[Category: Kries, H]]
<references/>
[[Category: O''Connor, S.E]]
__TOC__
[[Category: Basquin, J]]
</StructureSection>
[[Category: Aneurinibacillus migulanus]]
[[Category: Large Structures]]
[[Category: Basquin J]]
[[Category: Caputi L]]
[[Category: Kries H]]
[[Category: O'Connor SE]]
[[Category: Stephan P]]
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