Manipulation of an existing crystal form unexpectedly results in interwoven packing networks with pseudo-translational symmetry.
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 Asub subdomain. An attempt was made to take advantage of this packing by removing the Asub subdomain from the construct (F-AΔsub) 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.
['Reimer|Janice M|JM|', 'Aloise|Martin N|MN|', 'Powell|Harold R|HR|', 'Schmeing|T Martin|TM|']
D001426:Bacterial Proteins D058675:Brevibacillus D020134:Catalytic Domain D006096:Gramicidin D008958:Models, Molecular D010453:Peptide Synthases D017434:Protein Structure, Tertiary D013379:Substrate Specificity
pseudo-translational symmetry NRPS crystal packing formylation interwoven networks