Cations in human rhinoviruses.
All known crystal structures of rhinoviruses have some uninterpreted electron density on their fivefold axes at a distance of about 152 +/- 3 A from the viral center. This density had been assumed to be a Ca2+ ion, based on its shape, height, and the presence of Ca2+ ions in the crystallization solutions. Difference electron density maps between EGTA-soaked crystals of human rhinovirus 14 (HRV14), as well as HRV16, and their corresponding native structures show that this density is an EGTA-chelatable ion. Analysis of the coordination geometry indicates that the ions in HRV3, HRV14, and HRV1A could be Ca2+ and the ion in HRV16 might be Zn2+. These cations may play a role in regulation of rhinovirus stability, although the loss of the ion itself does not seem sufficient to lead to viral disassembly.
Zhao
R
R
Department of Biological Sciences, Purdue University, West Lafayette, Indiana, 47907-1392, USA.
Hadfield
A T
AT
Kremer
M J
MJ
Rossmann
M G
MG
D002118:Calcium / Q000032:analysis; D002412:Cations / Q000032:analysis*; D002614:Chelating Agents / Q000737:chemistry; D018360:Crystallography, X-Ray; D004533:Egtazic Acid / Q000737:chemistry; D004583:Electrons; D006801:Humans; D008670:Metals / Q000032:analysis; D011487:Protein Conformation; D012229:Rhinovirus / Q000737:chemistry* / Q000648:ultrastructure; D014764:Viral Proteins / Q000737:chemistry
D002412:Cations; D002614:Chelating Agents; D008670:Metals; D014764:Viral Proteins; D004533:Egtazic Acid; D002118:Calcium