Nature's favorite building block: Deciphering folding and capsid assembly of proteins with the HK97-fold

作者：Suhanovsky Margaret M; Teschke Carolyn M^*

来源：Virology, 2015, 479: 487-497.

DOI：10.1016/j.virol.2015.02.055

• HK97-fold
• Capsid protein structure
• Bacteriophage
• Coat protein
• Accessory domain

For many (if not all) bacterial and archaeal tailed viruses and eukaryotic Herpesvirdae the HK97-fold serves as the major architectural element in icosahedral capsid formation while still enabling the conformational flexibility required during assembly and maturation. Auxiliary proteins or Delta-domains strictly control assembly of multiple, identical, HK97-like subunits into procapsids with specific icosahedral symmetries, rather than aberrant non-icosahedral structures. Procapsids are precursor structures that mature into capsids in a process involving release of auxiliary proteins (or cleavage of Delta-domains), dsDNA packaging, and conformational rearrangement of the HK97-like subunits. Some coat proteins built on the ubiquitous HK97-fold also have accessory domains or loops that impart specific functions, such as increased monomer, procapsid, or capsid stability. In this review, we analyze the numerous HK97-like coat protein structures that are emerging in the literature (over 40 at time of writing) by comparing their topology, additional domains, and their assembly and misassembly reactions.

• 出版日期2015-5