rdf:type |
|
lifeskim:mentions |
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pubmed:issue |
5
|
pubmed:dateCreated |
2000-12-18
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pubmed:abstractText |
X-ray structures of the universal translation initiation factor IF2/eIF5B have been determined in three states: free enzyme, inactive IF2/eIF5B.GDP, and active IF2/eIF5B.GTP. The "chalice-shaped" enzyme is a GTPase that facilitates ribosomal subunit joining and Met-tRNA(i) binding to ribosomes in all three kingdoms of life. The conserved core of IF2/eIF5B consists of an N-terminal G domain (I) plus an EF-Tu-type beta barrel (II), followed by a novel alpha/beta/alpha-sandwich (III) connected via an alpha helix to a second EF-Tu-type beta barrel (IV). Structural comparisons reveal a molecular lever, which amplifies a modest conformational change in the Switch 2 region of the G domain induced by Mg(2+)/GTP binding over a distance of 90 A from the G domain active center to domain IV. Mechanisms of GTPase function and ribosome binding are discussed.
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pubmed:grant |
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Nov
|
pubmed:issn |
0092-8674
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pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:day |
22
|
pubmed:volume |
103
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
781-92
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pubmed:dateRevised |
2007-11-14
|
pubmed:meshHeading |
pubmed-meshheading:11114334-Amino Acid Motifs,
pubmed-meshheading:11114334-Amino Acid Sequence,
pubmed-meshheading:11114334-Binding Sites,
pubmed-meshheading:11114334-Crystallography, X-Ray,
pubmed-meshheading:11114334-Enzyme Activation,
pubmed-meshheading:11114334-Escherichia coli,
pubmed-meshheading:11114334-Eukaryotic Initiation Factor-5,
pubmed-meshheading:11114334-Guanine,
pubmed-meshheading:11114334-Guanosine Diphosphate,
pubmed-meshheading:11114334-Guanosine Triphosphate,
pubmed-meshheading:11114334-Methanococcus,
pubmed-meshheading:11114334-Models, Molecular,
pubmed-meshheading:11114334-Molecular Sequence Data,
pubmed-meshheading:11114334-Peptide Initiation Factors,
pubmed-meshheading:11114334-Protein Conformation,
pubmed-meshheading:11114334-Protein Structure, Secondary,
pubmed-meshheading:11114334-Protein Structure, Tertiary,
pubmed-meshheading:11114334-Sequence Homology, Amino Acid
|
pubmed:year |
2000
|
pubmed:articleTitle |
X-Ray structures of the universal translation initiation factor IF2/eIF5B: conformational changes on GDP and GTP binding.
|
pubmed:affiliation |
Laboratories of Molecular Biophysics The Rockefeller University 10021, New York, NY 10021, USA.
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
|