1IF0
PSEUDO-ATOMIC MODEL OF BACTERIOPHAGE HK97 PROCAPSID (PROHEAD II)
1IF0 の概要
エントリーDOI | 10.2210/pdb1if0/pdb |
関連するPDBエントリー | 1FH6 |
分子名称 | PROTEIN (MAJOR CAPSID PROTEIN GP5) (1 entity in total) |
機能のキーワード | bacteriophage, virus, capsid, cryoem, pseudo-atomic model., icosahedral virus |
由来する生物種 | Enterobacteria phage HK97 |
タンパク質・核酸の鎖数 | 7 |
化学式量合計 | 197958.25 |
構造登録者 | Conway, J.F.,Wikoff, W.R.,Cheng, N.,Duda, R.L.,Hendrix, R.W.,Johnson, J.E.,Steven, A.C. (登録日: 2001-04-11, 公開日: 2001-05-02, 最終更新日: 2024-02-07) |
主引用文献 | 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 Cited by 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: 11326105DOI: 10.1126/science.1058069 主引用文献が同じPDBエントリー |
実験手法 | ELECTRON MICROSCOPY (12 Å) |
構造検証レポート
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