6mg0: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
No edit summary
No edit summary
Line 3: Line 3:
<StructureSection load='6mg0' size='340' side='right'caption='[[6mg0]], [[Resolution|resolution]] 6.00&Aring;' scene=''>
<StructureSection load='6mg0' size='340' side='right'caption='[[6mg0]], [[Resolution|resolution]] 6.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6mg0]] 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=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>
<table><tr><td colspan='2'>[[6mg0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_10027 Atcc 10027]. 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 [https://proteopedia.org/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>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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='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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">lgrA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=54914 ATCC 10027])</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>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6mg0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mg0 OCA], [https://pdbe.org/6mg0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6mg0 RCSB], [https://www.ebi.ac.uk/pdbsum/6mg0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6mg0 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 ==
Line 19: Line 19:
</div>
</div>
<div class="pdbe-citations 6mg0" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 6mg0" style="background-color:#fffaf0;"></div>
==See Also==
*[[Linear gramicidin synthase|Linear gramicidin synthase]]
== References ==
== References ==
<references/>
<references/>

Revision as of 10:30, 29 June 2022

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

6mg0 is a 2 chain structure with sequence from Atcc 10027. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Gene:lgrA (ATCC 10027)
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

  1. 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

6mg0, resolution 6.00Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA