View source for 6mfy


==Crystal structure of a 5-domain construct of LgrA in the substrate donation state==
<StructureSection load='6mfy' size='340' side='right'caption='[[6mfy]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6mfy]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Brevibacillus_parabrevis Brevibacillus parabrevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MFY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6MFY 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=PNS:4-PHOSPHOPANTETHEINE'>PNS</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=6mfy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mfy OCA], [https://pdbe.org/6mfy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6mfy RCSB], [https://www.ebi.ac.uk/pdbsum/6mfy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6mfy ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/LGRA_BREPA LGRA_BREPA] Activates valine (or leucine, but much less frequently), and then glycine and catalyzes the formation of the peptide bond in the first step of peptide synthesis. This enzyme may also play a role in N-formylation of the first amino acid residue in the synthesized dipeptide.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Nonribosomal peptide synthetases (NRPSs) are biosynthetic enzymes that synthesize natural product therapeutics using a modular synthetic logic, whereby each module adds one aminoacyl substrate to the nascent peptide. We have determined five x-ray crystal structures of large constructs of the NRPS linear gramicidin synthetase, including a structure of a full core dimodule in conformations organized for the condensation reaction and intermodular peptidyl substrate delivery. The structures reveal differences in the relative positions of adjacent modules, which are not strictly coupled to the catalytic cycle and are consistent with small-angle x-ray scattering data. The structures and covariation analysis of homologs allowed us to create mutants that improve the yield of a peptide from a module-swapped dimodular NRPS.

Structures of a dimodular nonribosomal peptide synthetase reveal conformational flexibility.,Reimer JM, Eivaskhani M, Harb I, Guarne A, Weigt M, Schmeing TM Science. 2019 Nov 8;366(6466). pii: 366/6466/eaaw4388. doi:, 10.1126/science.aaw4388. PMID:31699907<ref>PMID:31699907</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6mfy" style="background-color:#fffaf0;"></div>

==See Also==
*[[Linear gramicidin synthase|Linear gramicidin synthase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Brevibacillus parabrevis]]
[[Category: Large Structures]]
[[Category: Eivaskhani M]]
[[Category: Harb I]]
[[Category: Reimer JM]]
[[Category: Schmeing TM]]