Manipulation of an existing crystal form unexpectedly results in interwoven packing networks with pseudo-translational symmetry.

ABSTRACT: Nonribosomal 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_Δsub) 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 secon

SUBMITTER: Reimer JM 

PROVIDER: S-EPMC5053139 | biostudies-literature | 2016 Oct

REPOSITORIES: biostudies-literature