8p5o: Difference between revisions
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==Proline activating adenylation domain of gramicidin S synthetase 2 - GrsB1-Acore== | |||
<StructureSection load='8p5o' size='340' side='right'caption='[[8p5o]], [[Resolution|resolution]] 2.60Å' 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]] 2.6Å</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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 8p5o" style="background-color:#fffaf0;"></div> | ||
[[Category: Caputi | == References == | ||
[[Category: Kries | <references/> | ||
[[Category: O | __TOC__ | ||
[[Category: | </StructureSection> | ||
[[Category: Aneurinibacillus migulanus]] | |||
[[Category: Large Structures]] | |||
[[Category: Basquin J]] | |||
[[Category: Caputi L]] | |||
[[Category: Kries H]] | |||
[[Category: O'Connor SE]] | |||
[[Category: Stephan P]] | |||
Revision as of 08:47, 5 July 2023
Proline activating adenylation domain of gramicidin S synthetase 2 - GrsB1-AcoreProline activating adenylation domain of gramicidin S synthetase 2 - GrsB1-Acore
Structural highlights
FunctionGRSB_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. Publication Abstract from PubMedEngineering 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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