2m5s

Publication Abstract from PubMed

Some capsid proteins built on the ubiquitous HK97-fold have accessory domains imparting specific functions. Bacteriophage P22 coat protein has a unique insertion domain (I-domain). Two prior I-domain models from subnanometer cryoelectron microscopy (cryoEM) reconstructions differed substantially. Therefore, the I-domain's nuclear magnetic resonance structure was determined and also used to improve cryoEM models of coat protein. The I-domain has an antiparallel six-stranded beta-barrel fold, not previously observed in HK97-fold accessory domains. The D-loop, which is dynamic in the isolated I-domain and intact monomeric coat protein, forms stabilizing salt bridges between adjacent capsomers in procapsids. The S-loop is important for capsid size determination, likely through intrasubunit interactions. Ten of 18 coat protein temperature-sensitive-folding substitutions are in the I-domain, indicating its importance in folding and stability. Several are found on a positively charged face of the beta-barrel that anchors the I-domain to a negatively charged surface of the coat protein HK97-core.

Multiple Functional Roles of the Accessory I-Domain of Bacteriophage P22 Coat Protein Revealed by NMR Structure and CryoEM Modeling.,Rizzo AA, Suhanovsky MM, Baker ML, Fraser LC, Jones LM, Rempel DL, Gross ML, Chiu W, Alexandrescu AT, Teschke CM Structure. 2014 Jun 10;22(6):830-41. doi: 10.1016/j.str.2014.04.003. Epub 2014, May 15. PMID:24836025^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.