1IF0

PSEUDO-ATOMIC MODEL OF BACTERIOPHAGE HK97 PROCAPSID (PROHEAD II)

Summary for 1IF0

• Entry DOI: 10.2210/pdb1if0/pdb
• Related: 1FH6
• Descriptor: PROTEIN (MAJOR CAPSID PROTEIN GP5) (1 entity in total)
• Functional Keywords: bacteriophage, virus, capsid, cryoem, pseudo-atomic model., icosahedral virus
• Biological source: Enterobacteria phage HK97
• Total number of polymer chains: 7
• Total formula weight: 197958.25

Authors

Conway, J.F.,Wikoff, W.R.,Cheng, N.,Duda, R.L.,Hendrix, R.W.,Johnson, J.E.,Steven, A.C. (deposition date: 2001-04-11, release date: 2001-05-02, Last modification date: 2024-02-07)

Primary citation

Conway, J.F.,Wikoff, W.R.,Cheng, N.,Duda, R.L.,Hendrix, R.W.,Johnson, J.E.,Steven, A.C.
Virus maturation involving large subunit rotations and local refolding.
Science, 292:744-748, 2001

PubMed Abstract: Large-scale conformational changes transform viral precursors into infectious virions. The structure of bacteriophage HK97 capsid, Head-II, was recently solved by crystallography, revealing a catenated cross-linked topology. We have visualized its precursor, Prohead-II, by cryoelectron microscopy and modeled the conformational change by appropriately adapting Head-II. Rigid-body rotations ( approximately 40 degrees) cause switching to an entirely different set of interactions; in addition, two motifs undergo refolding. These changes stabilize the capsid by increasing the surface area buried at interfaces and bringing the cross-link-forming residues, initially approximately 40 angstroms apart, close together. The inner surface of Prohead-II is negatively charged, suggesting that the transition is triggered electrostatically by DNA packaging.

PubMed: 11326105
DOI: 10.1126/science.1058069

Experimental method

ELECTRON MICROSCOPY (12 Å)