7c1h: Difference between revisions
New page: '''Unreleased structure''' The entry 7c1h is ON HOLD Authors: Description: Category: Unreleased Structures |
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==Crystal structure of the starter condensation domain of rhizomide synthetase RzmA== | |||
<StructureSection load='7c1h' size='340' side='right'caption='[[7c1h]], [[Resolution|resolution]] 2.30Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7c1h]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycetohabitans_rhizoxinica_HKI_454 Mycetohabitans rhizoxinica HKI 454]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7C1H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7C1H 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]] 2.3Å</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=7c1h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7c1h OCA], [https://pdbe.org/7c1h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7c1h RCSB], [https://www.ebi.ac.uk/pdbsum/7c1h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7c1h ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/E5ATN9_MYCRK E5ATN9_MYCRK] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Nonribosomal peptide synthetases containing starter condensation domains direct the biosynthesis of nonribosomal lipopeptides, which generally exhibit wide bioactivities. The acyl chain has strong impacts on bioactivity and toxicity, but the lack of an in-depth understanding of starter condensation domain-mediated lipoinitiation limits the bioengineering of NRPSs to obtain novel derivatives with desired acyl chains. Here, we show that the acyl chains of the lipopeptides rhizomide, holrhizin, and glidobactin were modified by engineering the starter condensation domain, suggesting a workable approach to change the acyl chain. Based on the structure of the mutated starter condensation domain of rhizomide biosynthetic enzyme RzmA in complex with octanoyl-CoA and related point mutation experiments, we identify a set of residues responsible for the selectivity of substrate acyl chains and extend the acyl chains from acetyl to palmitoyl. Furthermore, we illustrate three possible conformational states of starter condensation domains during the reaction cycle of the lipoinitiation process. Our studies provide further insights into the mechanism of lipoinitiation and the engineering of nonribosomal peptide synthetases. | |||
Engineering and elucidation of the lipoinitiation process in nonribosomal peptide biosynthesis.,Zhong L, Diao X, Zhang N, Li F, Zhou H, Chen H, Bai X, Ren X, Zhang Y, Wu D, Bian X Nat Commun. 2021 Jan 12;12(1):296. doi: 10.1038/s41467-020-20548-8. PMID:33436600<ref>PMID:33436600</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 7c1h" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Mycetohabitans rhizoxinica HKI 454]] | |||
[[Category: Bian X]] | |||
[[Category: Chen HN]] | |||
[[Category: Diao X]] | |||
[[Category: Li FW]] | |||
[[Category: Ren X]] | |||
[[Category: Wu D]] | |||
[[Category: Zhang N]] | |||
[[Category: Zhang Y]] | |||
[[Category: Zhong L]] | |||
[[Category: Zhou HB]] | |||
Latest revision as of 18:49, 29 November 2023
Crystal structure of the starter condensation domain of rhizomide synthetase RzmACrystal structure of the starter condensation domain of rhizomide synthetase RzmA
Structural highlights
FunctionPublication Abstract from PubMedNonribosomal peptide synthetases containing starter condensation domains direct the biosynthesis of nonribosomal lipopeptides, which generally exhibit wide bioactivities. The acyl chain has strong impacts on bioactivity and toxicity, but the lack of an in-depth understanding of starter condensation domain-mediated lipoinitiation limits the bioengineering of NRPSs to obtain novel derivatives with desired acyl chains. Here, we show that the acyl chains of the lipopeptides rhizomide, holrhizin, and glidobactin were modified by engineering the starter condensation domain, suggesting a workable approach to change the acyl chain. Based on the structure of the mutated starter condensation domain of rhizomide biosynthetic enzyme RzmA in complex with octanoyl-CoA and related point mutation experiments, we identify a set of residues responsible for the selectivity of substrate acyl chains and extend the acyl chains from acetyl to palmitoyl. Furthermore, we illustrate three possible conformational states of starter condensation domains during the reaction cycle of the lipoinitiation process. Our studies provide further insights into the mechanism of lipoinitiation and the engineering of nonribosomal peptide synthetases. Engineering and elucidation of the lipoinitiation process in nonribosomal peptide biosynthesis.,Zhong L, Diao X, Zhang N, Li F, Zhou H, Chen H, Bai X, Ren X, Zhang Y, Wu D, Bian X Nat Commun. 2021 Jan 12;12(1):296. doi: 10.1038/s41467-020-20548-8. PMID:33436600[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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