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| | <StructureSection load='6mfz' size='340' side='right'caption='[[6mfz]], [[Resolution|resolution]] 6.00Å' scene=''> | | <StructureSection load='6mfz' size='340' side='right'caption='[[6mfz]], [[Resolution|resolution]] 6.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6mfz]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_10027 Atcc 10027]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MFZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6MFZ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6mfz]] is a 2 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=6MFZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6MFZ FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PNS:4-PHOSPHOPANTETHEINE'>PNS</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 6Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">lgrA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=54914 ATCC 10027])</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></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=6mfz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mfz OCA], [http://pdbe.org/6mfz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6mfz RCSB], [http://www.ebi.ac.uk/pdbsum/6mfz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6mfz ProSAT]</span></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=6mfz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mfz OCA], [https://pdbe.org/6mfz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6mfz RCSB], [https://www.ebi.ac.uk/pdbsum/6mfz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6mfz ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == 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. | + | [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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 6mfz" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6mfz" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Linear gramicidin synthase|Linear gramicidin synthase]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 10027]] | + | [[Category: Brevibacillus parabrevis]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Eivaskhani, M]] | + | [[Category: Eivaskhani M]] |
| - | [[Category: Harb, I]] | + | [[Category: Harb I]] |
| - | [[Category: Reimer, J M]] | + | [[Category: Reimer JM]] |
| - | [[Category: Schmeing, T M]] | + | [[Category: Schmeing TM]] |
| - | [[Category: Enzyme]]
| + | |
| - | [[Category: Ligase]]
| + | |
| - | [[Category: Linear gramicidin]]
| + | |
| - | [[Category: Natural product]]
| + | |
| - | [[Category: Nonribosomal peptide synthetase]]
| + | |
| - | [[Category: Nrp]]
| + | |
| - | [[Category: Tailoring domain]]
| + | |
| 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 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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Reimer JM, Eivaskhani M, Harb I, Guarne A, Weigt M, Schmeing TM. Structures of a dimodular nonribosomal peptide synthetase reveal conformational flexibility. Science. 2019 Nov 8;366(6466). pii: 366/6466/eaaw4388. doi:, 10.1126/science.aaw4388. PMID:31699907 doi:http://dx.doi.org/10.1126/science.aaw4388
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