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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
13
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pubmed:dateCreated |
2005-3-30
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pubmed:abstractText |
We used cryo-electron tomography in conjunction with single-particle averaging techniques to study the structures of frozen-hydrated envelope glycoprotein (Env) complexes on intact Moloney murine leukemia retrovirus particles. Cryo-electron tomography allows 3D imaging of viruses in toto at a resolution sufficient to locate individual macromolecules, and local averaging of abundant complexes substantially improves the resolution. The averaging of repetitive features in electron tomograms is hampered by a low signal-to-noise ratio and anisotropic resolution, which results from the "missing-wedge" effect. We developed an iterative 3D averaging algorithm that compensates for this effect and used it to determine the trimeric structure of Env to a resolution of 2.7 nm, at which individual domains can be resolved. Strikingly, the 3D reconstruction is shaped like a tripod in which the trimer penetrates the membrane at three distinct locations approximately 4.5 nm apart from one another. The Env reconstruction allows tentative docking of the x-ray crystal structure of the receptor-binding domain. This study thus provides 3D structural information regarding the prefusion conformation of an intact unstained retrovirus surface protein.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/15774580-10200260,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15774580-10684305,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15774580-10944528,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15774580-11012823,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15774580-11286892,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/15774580-11395423,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15774580-11472084,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15774580-11566128,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15774580-11722164,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15774580-11752436,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15774580-11988472,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/15774580-12704429,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15774580-12892723,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15774580-14631040,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15774580-14633978,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15774580-14668432,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15774580-14963166,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/15774580-8612078,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15774580-8743704,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15774580-9108481,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/15774580-9636143,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15774580-9641677,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15774580-9707417
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
29
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pubmed:volume |
102
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
4729-34
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pubmed:dateRevised |
2010-9-21
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pubmed:meshHeading |
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pubmed:year |
2005
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pubmed:articleTitle |
Retrovirus envelope protein complex structure in situ studied by cryo-electron tomography.
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pubmed:affiliation |
Abteilung für Molekulare Strukturbiologie, Max-Planck-Institut für Biochemie, Am Klopferspitz 18, D-82152 Martinsried, Germany. foerster@biochem.mpg.de
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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