2FSY
Bacteriophage HK97 Pepsin-treated Expansion Intermediate IV
Summary for 2FSY
Entry DOI | 10.2210/pdb2fsy/pdb |
Related | 2FRP 2FS3 2FT1 2FTE |
Descriptor | major capsid protein (1 entity in total) |
Functional Keywords | bacteriophage, hk97, capsid protein, expansion intermediate, icosahedral virus, virus |
Biological source | Enterobacteria phage HK97 |
Cellular location | Virion: P49861 |
Total number of polymer chains | 7 |
Total formula weight | 215632.25 |
Authors | Gan, L.,Speir, J.A.,Conway, J.F.,Lander, G.,Cheng, N.,Firek, B.A.,Hendrix, R.W.,Duda, R.L.,Liljas, L.,Johnson, J.E. (deposition date: 2006-01-23, release date: 2006-02-07, Last modification date: 2023-09-20) |
Primary citation | Gan, L.,Speir, J.A.,Conway, J.F.,Lander, G.,Cheng, N.,Firek, B.A.,Hendrix, R.W.,Duda, R.L.,Liljas, L.,Johnson, J.E. Capsid Conformational Sampling in HK97 Maturation Visualized by X-Ray Crystallography and Cryo-EM. Structure, 14:1655-1665, 2006 Cited by PubMed Abstract: Maturation of the bacteriophage HK97 capsid from a precursor (Prohead II) to the mature state (Head II) involves a 60 A radial expansion. The mature particle is formed by 420 copies of the major capsid protein organized on a T = 7 laevo lattice with each subunit covalently crosslinked to two neighbors. Well-characterized pH 4 expansion intermediates make HK97 valuable for investigating quaternary structural dynamics. Here, we use X-ray crystallography and cryo-EM to demonstrate that in the final transition in maturation (requiring neutral pH), pentons in Expansion Intermediate IV (EI-IV) reversibly sample 14 A translations and 6 degrees rotations relative to a fixed hexon lattice. The limit of this trajectory corresponds to the Head II conformation that is secured at this extent only by the formation of the final class of covalent crosslinks. Mutants that cannot crosslink or EI-IV particles that have been rendered incapable of forming the final crosslink remain in the EI-IV state. PubMed: 17098191DOI: 10.1016/j.str.2006.09.006 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (3.8 Å) |
Structure validation
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