Unknown

Dataset Information

0

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


ABSTRACT: 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 ?-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 ?-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.

SUBMITTER: Suhanovsky MM 

PROVIDER: S-EPMC4424165 | biostudies-literature | 2015 May

REPOSITORIES: biostudies-literature

altmetric image

Publications

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

Suhanovsky Margaret M MM   Teschke Carolyn M CM  

Virology 20150408


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 Δ-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 st  ...[more]

Similar Datasets

| S-EPMC2938056 | biostudies-literature
| S-EPMC4044616 | biostudies-literature
| S-EPMC1941702 | biostudies-literature
| S-EPMC4020191 | biostudies-literature
| S-EPMC2840706 | biostudies-literature
| S-EPMC6626583 | biostudies-literature
| S-EPMC5584385 | biostudies-literature
| S-EPMC7756758 | biostudies-literature
| S-EPMC10015872 | biostudies-literature
| S-EPMC3738745 | biostudies-literature