View source for 8jbr


==Structure of McyA2-CAPCP==
<StructureSection load='8jbr' size='340' side='right'caption='[[8jbr]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8jbr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Microcystis_aeruginosa_PCC_7806 Microcystis aeruginosa PCC 7806]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8JBR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8JBR 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]] 2.5&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=PNS:4-PHOSPHOPANTETHEINE'>PNS</scene></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=8jbr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8jbr OCA], [https://pdbe.org/8jbr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8jbr RCSB], [https://www.ebi.ac.uk/pdbsum/8jbr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8jbr ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A8YJV7_MICA7 A8YJV7_MICA7] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Nonribosomal peptide synthetases (NRPSs) are large multidomain enzymes for the synthesis of a variety of bioactive peptides in a modular and pipelined fashion. Here, we investigated how the condensation (C) domain and the adenylation (A) domain cooperate with each other for the efficient catalytic activity in microcystin NRPS modules. We solved two crystal structures of the microcystin NRPS modules, representing two different conformations in the NRPS catalytic cycle. Our data reveal that the dynamic interaction between the C and the A domains in these modules is mediated by the conserved "RXGR" motif, and this interaction is important for the adenylation activity. Furthermore, the "RXGR" motif-mediated dynamic interaction and its functional regulation are prevalent in different NRPSs modules possessing both the A and the C domains. This study provides new insights into the catalytic mechanism of NRPSs and their engineering strategy for synthetic peptides with different structures and properties.

Modular catalytic activity of nonribosomal peptide synthetases depends on the dynamic interaction between adenylation and condensation domains.,Peng YJ, Chen Y, Zhou CZ, Miao W, Jiang YL, Zeng X, Zhang CC Structure. 2024 Apr 4;32(4):440-452.e4. doi: 10.1016/j.str.2024.01.010. Epub 2024 , Feb 9. PMID:38340732<ref>PMID:38340732</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8jbr" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Microcystis aeruginosa PCC 7806]]
[[Category: Peng YJ]]