Structural highlights
Function
[DNIV_BPMU] This protein catalyzes the inversion of a 3000-bp segment of phage DNA. The inversion results in a modification of the 3'-end of the tail fiber gene and alters the host specificity.
Publication Abstract from PubMed
Crystals of the G-segment invertase in complex with a 37-base-pair asymmetric DNA duplex substrate had an unusually high solvent content of 88% and diffracted to a maximal resolution of about 5.0 A. These crystals exhibited a high degree of non-isomorphism and anisotropy, which presented a serious challenge for structure determination by isomorphous replacement. Here, a procedure of cross-crystal averaging is described that uses large non-isomorphous crystallographic data with a priori information of an approximate molecular boundary as determined from a minimal amount of experimental phase information. Using this procedure, high-quality experimental phases were obtained that have enabled it to be shown that the conformation of the bound substrate DNA duplex significantly differs from those of substrates bound in other serine recombinase-DNA complexes.
Exploiting large non-isomorphous differences for phase determination of a G-segment invertase-DNA complex.,Ritacco CJ, Steitz TA, Wang J Acta Crystallogr D Biol Crystallogr. 2014 Mar;70(Pt 3):685-93. doi:, 10.1107/S1399004713032392. Epub 2014 Feb 15. PMID:24598738[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Ritacco CJ, Steitz TA, Wang J. Exploiting large non-isomorphous differences for phase determination of a G-segment invertase-DNA complex. Acta Crystallogr D Biol Crystallogr. 2014 Mar;70(Pt 3):685-93. doi:, 10.1107/S1399004713032392. Epub 2014 Feb 15. PMID:24598738 doi:http://dx.doi.org/10.1107/S1399004713032392
