We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

6mfx

From Proteopedia

Jump to: navigation, search

Crystal structure of a 4-domain construct of a mutant of LgrA in the substrate donation state

Structural highlights

6mfx is a 1 chain structure with sequence from Brevibacillus parabrevis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.2Å
Ligands:	, ,
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.

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