6mg0: Difference between revisions
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==Crystal structure of a 5-domain construct of LgrA in the thiolation state== | |||
<StructureSection load='6mg0' size='340' side='right'caption='[[6mg0]], [[Resolution|resolution]] 6.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6mg0]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MG0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6MG0 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DG9:5-({[(2R,3R)-3-AMINO-2-{[2-({N-[(2R)-2-HYDROXY-3,3-DIMETHYL-4-{[OXIDO(OXO)PHOSPHONIO]OXY}BUTANOYL]-BETA-ALANYL}AMINO)ETHYL]SULFANYL}-4-METHYLPENTYL]SULFONYL}AMINO)-5-DEOXYADENOSINE'>DG9</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6mg0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mg0 OCA], [http://pdbe.org/6mg0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6mg0 RCSB], [http://www.ebi.ac.uk/pdbsum/6mg0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6mg0 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6mg0" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Eivaskhani, M]] | |||
[[Category: Harb, I]] | |||
[[Category: Reimer, J M]] | |||
[[Category: Schmeing, T M]] | |||
[[Category: Enzyme]] | |||
[[Category: Ligase]] | |||
[[Category: Linear gramicidin]] | |||
[[Category: Natural product]] | |||
[[Category: Nonribosomal peptide synthetase]] | |||
[[Category: Nrp]] | |||
[[Category: Tailoring domain]] | |||
Revision as of 18:24, 20 November 2019
Crystal structure of a 5-domain construct of LgrA in the thiolation stateCrystal structure of a 5-domain construct of LgrA in the thiolation state
Structural highlights
Function[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. Publication Abstract from PubMedNonribosomal 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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