EMDB/PDB/SASBDBから引用されている文献のデータベース

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構造解析手法	All X線回折 NMR 電子顕微鏡小角散乱中性子線回折線維回折粉末回折赤外分光 EPR FRET 理論モデルハイブリッド
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IF	>30 >20 >10 >5 all

タイトル	Structure of the pseudorabies virus capsid: comparison with herpes simplex virus type 1 and differential binding of essential minor proteins.
ジャーナル・号・ページ	J Mol Biol, Vol. 425, Issue 18, Page 3415-3428, Year 2013
掲載日	2013年9月23日
著者	F L Homa / J B Huffman / K Toropova / H R Lopez / A M Makhov / J F Conway /
PubMed 要旨	The structure of pseudorabies virus (PRV) capsids isolated from the nucleus of infected cells and from PRV virions was determined by cryo-electron microscopy (cryo-EM) and compared to herpes simplex ...The structure of pseudorabies virus (PRV) capsids isolated from the nucleus of infected cells and from PRV virions was determined by cryo-electron microscopy (cryo-EM) and compared to herpes simplex virus type 1 (HSV-1) capsids. PRV capsid structures closely resemble those of HSV-1, including distribution of the capsid vertex specific component (CVSC) of HSV-1, which is a heterodimer of the pUL17 and pUL25 proteins. Occupancy of CVSC on all PRV capsids is near 100%, compared to ~50% reported for HSV-1 C-capsids and 25% or less that we measure for HSV-1 A- and B-capsids. A PRV mutant lacking pUL25 does not produce C-capsids and lacks visible CVSC density in the cryo-EM-based reconstruction. A reconstruction of PRV capsids in which green fluorescent protein was fused within the N-terminus of pUL25 confirmed previous studies with a similar HSV-1 capsid mutant localizing pUL25 to the CVSC density region that is distal to the penton. However, comparison of the CVSC density in a 9-Å-resolution PRV C-capsid map with the available crystal structure of HSV-1 pUL25 failed to find a satisfactory fit, suggesting either a different fold for PRV pUL25 or a capsid-bound conformation for pUL25 that does not match the X-ray model determined from protein crystallized in solution. The PRV capsid imaged within virions closely resembles C-capsids with the addition of weak but significant density shrouding the pentons that we attribute to tegument proteins. Our results demonstrate significant structure conservation between the PRV and HSV capsids.
リンク	J Mol Biol / PubMed:23827137 / PubMed Central
手法	EM (単粒子)
解像度	9.0 - 23.2 Å
構造データ	EMDB-5650: Pseudorabies virus C-capsid from cryo-electron microscopy 手法: EM (単粒子) / 解像度: 9.0 Å EMDB-5652: Pseudorabies virus B-capsid from cryo-electron microscopy 手法: EM (単粒子) / 解像度: 15.9 Å EMDB-5654: Pseudorabies virus A-capsid from cryo-electron microscopy 手法: EM (単粒子) / 解像度: 14.1 Å EMDB-5655: Pseudorabies virus virion capsid from cryo-electron microscopy 手法: EM (単粒子) / 解像度: 22.6 Å EMDB-5656: Pseudorabies GS-2168 B-capsid from cryo-electron microscopy 手法: EM (単粒子) / 解像度: 14.7 Å EMDB-5657: Structure of the pseudorabies virus capsid: comparison with herpes simplex virus type 1 and differential binding of essential minor proteins 手法: EM (単粒子) / 解像度: 23.2 Å EMDB-5659: Cryo-electron microscopy of herpesvirus simplex type 1 C-capsid 手法: EM (単粒子) / 解像度: 16.7 Å EMDB-5660: Cryo-electron microscopy of herpesvirus simplex type 1 B-capsid 手法: EM (単粒子) / 解像度: 16.9 Å EMDB-5661: Cryo-electron microscopy of herpesvirus simplex type 1 A-capsid 手法: EM (単粒子) / 解像度: 16.9 Å