1rqv
From Proteopedia
(New page: 200px<br /><applet load="1rqv" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rqv" /> '''Spatial model of L7 dimer from E.coli with o...) |
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| - | [[Image:1rqv.gif|left|200px]]<br /><applet load="1rqv" size=" | + | [[Image:1rqv.gif|left|200px]]<br /><applet load="1rqv" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1rqv" /> | caption="1rqv" /> | ||
'''Spatial model of L7 dimer from E.coli with one hinge region in helical state'''<br /> | '''Spatial model of L7 dimer from E.coli with one hinge region in helical state'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Based on the (1)H-(15)N NMR spectroscopy data, the three-dimensional | + | 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== | ==About this Structure== | ||
| - | 1RQV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http:// | + | 1RQV is a [http://en.wikipedia.org/wiki/Single_protein 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=1RQV OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Arseniev, A | + | [[Category: Arseniev, A S.]] |
| - | [[Category: Bocharov, E | + | [[Category: Bocharov, E V.]] |
| - | [[Category: Gudkov, A | + | [[Category: Gudkov, A T.]] |
| - | [[Category: Jaravine, V | + | [[Category: Jaravine, V A.]] |
| - | [[Category: Korzhnev, D | + | [[Category: Korzhnev, D M.]] |
| - | [[Category: Pavlov, K | + | [[Category: Pavlov, K V.]] |
| - | [[Category: Sobol, A | + | [[Category: Sobol, A G.]] |
[[Category: nmr]] | [[Category: nmr]] | ||
[[Category: protein l7/l12]] | [[Category: protein l7/l12]] | ||
[[Category: ribosome]] | [[Category: ribosome]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:53:39 2008'' |
Revision as of 12:53, 21 February 2008
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Spatial model of L7 dimer from E.coli with one hinge region in helical state
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
1RQV 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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