1OHG

STRUCTURE OF THE DSDNA BACTERIOPHAGE HK97 MATURE EMPTY CAPSID

Replaces:  1FH6

Summary for 1OHG

• Entry DOI: 10.2210/pdb1ohg/pdb
• Related: 1IF0
• Descriptor: MAJOR CAPSID PROTEIN, SULFATE ION, CHLORIDE ION (3 entities in total)
• Functional Keywords: virus, virus coat protein, virus/viral protein, bacteriophage, capsid, auto- catalytic cross-link, icosahedral virus
• Biological source: BACTERIOPHAGE HK97
• Cellular location: Virion (Potential): P49861
• Total number of polymer chains: 7
• Total formula weight: 215763.77

Authors

Helgstrand, C.,Wikoff, W.R.,Duda, R.L.,Hendrix, R.W.,Johnson, J.E.,Liljas, L. (deposition date: 2003-05-26, release date: 2003-12-11, Last modification date: 2024-05-01)

Primary citation

Helgstrand, C.,Wikoff, W.R.,Duda, R.L.,Hendrix, R.W.,Johnson, J.E.,Liljas, L.
The Refined Structure of a Protein Catenane: The Hk97 Bacteriophage Capsid at 3.44A Resolution
J.Mol.Biol., 334:885-, 2003

PubMed Abstract: The HK97 bacteriophage capsid is a unique example of macromolecular catenanes: interlocked rings of covalently attached protein subunits. The chain mail organization of the subunits stabilizes a particle in which the maximum thickness of the protein shell is 18A and the maximum diameter is 550A. The electron density has the appearance of a balloon illustrating the extraordinary strength conferred by the unique subunit organization. The refined structure shows novel qualities of the HK97 shell protein, gp5 that, together with the protease gp4, guides the assembly and maturation of the virion. Although gp5 forms hexamers and pentamers and the subunits exist in different structural environments, the tertiary structures of the seven protein molecules in the viral asymmetric unit are closely similar. The interactions of the subunits in the shell are exceptionally complex with each subunit interacting with nine other subunits. The interactions of the N-terminus released after gp5 cleavage appear important for organization of the loops that become crosslinked to the core of a neighboring subunit at the maturation. A comparison with a model of the Prohead II structure revealed that the surfaces of non-covalent contact between the monomers that build up hexamers/pentamers are completely redefined during maturation.

PubMed: 14643655
DOI: 10.1016/J.JMB.2003.09.035

Experimental method

X-RAY DIFFRACTION (3.45 Å)