View source for 8hlk


==Structure of McyB-C1A1 complexed with L-Leu and AMP==
<StructureSection load='8hlk' size='340' side='right'caption='[[8hlk]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8hlk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Microcystis_aeruginosa Microcystis aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8HLK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8HLK 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]] 2.7&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=LEU:LEUCINE'>LEU</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=8hlk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8hlk OCA], [https://pdbe.org/8hlk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8hlk RCSB], [https://www.ebi.ac.uk/pdbsum/8hlk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8hlk ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/O54504_MICAE O54504_MICAE] 
<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 8hlk" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Microcystis aeruginosa]]
[[Category: Peng YJ]]