1rqu
From Proteopedia
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| - | [[Image:1rqu.gif|left|200px]] | + | [[Image:1rqu.gif|left|200px]] |
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| - | '''NMR structure of L7 dimer from E.coli''' | + | {{Structure |
| + | |PDB= 1rqu |SIZE=350|CAPTION= <scene name='initialview01'>1rqu</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''NMR structure of L7 dimer from E.coli''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1RQU is a [ | + | 1RQU is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RQU OCA]. |
==Reference== | ==Reference== | ||
| - | From structure and dynamics of protein L7/L12 to molecular switching in ribosome., Bocharov EV, Sobol AG, Pavlov KV, Korzhnev DM, Jaravine VA, Gudkov AT, Arseniev AS, J Biol Chem. 2004 Apr 23;279(17):17697-706. Epub 2004 Feb 11. PMID:[http:// | + | From structure and dynamics of protein L7/L12 to molecular switching in ribosome., Bocharov EV, Sobol AG, Pavlov KV, Korzhnev DM, Jaravine VA, Gudkov AT, Arseniev AS, J Biol Chem. 2004 Apr 23;279(17):17697-706. Epub 2004 Feb 11. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14960595 14960595] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: ribosome]] | [[Category: ribosome]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:55:07 2008'' |
Revision as of 11:55, 20 March 2008
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NMR structure of L7 dimer from E.coli
Overview
Based on the (1)H-(15)N NMR spectroscopy data, the three-dimensional structure and internal dynamic properties of ribosomal protein L7 from Escherichia coli were derived. The structure of L7 dimer in solution can be described as a set of three distinct domains, tumbling rather independently and linked via flexible hinge regions. The dimeric N-terminal domain (residues 1-32) consists of two antiparallel alpha-alpha-hairpins forming a symmetrical four-helical bundle, whereas the two identical C-terminal domains (residues 52-120) adopt a compact alpha/beta-fold. There is an indirect evidence of the existence of transitory helical structures at least in the first part (residues 33-43) of the hinge region. Combining structural data for the ribosomal protein L7/L12 from NMR spectroscopy and x-ray crystallography, it was suggested that its hinge region acts as a molecular switch, initiating "ratchet-like" motions of the L7/L12 stalk with respect to the ribosomal surface in response to elongation factor binding and GTP hydrolysis. This hypothesis allows an explanation of events observed during the translation cycle and provides useful insights into the role of protein L7/L12 in the functioning of the ribosome.
About this Structure
1RQU is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
From structure and dynamics of protein L7/L12 to molecular switching in ribosome., Bocharov EV, Sobol AG, Pavlov KV, Korzhnev DM, Jaravine VA, Gudkov AT, Arseniev AS, J Biol Chem. 2004 Apr 23;279(17):17697-706. Epub 2004 Feb 11. PMID:14960595
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