5jnf
From Proteopedia
Crystal structure of the LgrA initiation module excluding the Asub domain: F-A-delta-sub
Structural highlights
FunctionLGRA_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 multimodular enzymes that synthesize a myriad of diverse molecules. Tailoring domains have been co-opted into NRPSs to introduce further variety into nonribosomal peptide products. Linear gramicidin synthetase contains a unique formylation-tailoring domain in its initiation module (F-A-PCP). The structure of the F-A di-domain has previously been determined in a crystal form which had large solvent channels and no density for the minor A(sub) subdomain. An attempt was made to take advantage of this packing by removing the A(sub) subdomain from the construct (F-A(Deltasub)) in order to produce a crystal that could accommodate the PCP domain. In the resulting crystal the original packing network was still present, but a second network with the same packing and almost no contact with the original network took the place of the solvent channels and changed the space group of the crystal. Manipulation of an existing crystal form unexpectedly results in interwoven packing networks with pseudo-translational symmetry.,Reimer JM, Aloise MN, Powell HR, Schmeing TM Acta Crystallogr D Struct Biol. 2016 Oct 1;72(Pt 10):1130-1136. doi: , 10.1107/S2059798316013504. Epub 2016 Sep 20. PMID:27710934[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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