1g7s: Difference between revisions
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|PDB= 1g7s |SIZE=350|CAPTION= <scene name='initialview01'>1g7s</scene>, resolution 2.Å | |PDB= 1g7s |SIZE=350|CAPTION= <scene name='initialview01'>1g7s</scene>, resolution 2.Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=GDP:GUANOSINE-5 | |LIGAND= <scene name='pdbligand=GDP:GUANOSINE-5'-DIPHOSPHATE'>GDP</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
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[[Category: translational gtpase]] | [[Category: translational gtpase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 11:53:42 2008'' | ||
Revision as of 12:53, 23 March 2008
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X-RAY STRUCTURE OF TRANSLATION INITIATION FACTOR IF2/EIF5B COMPLEXED WITH GDP
OverviewOverview
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.
About this StructureAbout this Structure
1G7S is a Single protein structure of sequence from Methanothermobacter thermautotrophicus. Full crystallographic information is available from OCA.
ReferenceReference
X-Ray structures of the universal translation initiation factor IF2/eIF5B: conformational changes on GDP and GTP binding., Roll-Mecak A, Cao C, Dever TE, Burley SK, Cell. 2000 Nov 22;103(5):781-92. PMID:11114334
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