1n88
From Proteopedia
(New page: 200px<br /><applet load="1n88" size="450" color="white" frame="true" align="right" spinBox="true" caption="1n88" /> '''NMR structure of the ribosomal protein L23 f...) |
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'''NMR structure of the ribosomal protein L23 from Thermus thermophilus.'''<br /> | '''NMR structure of the ribosomal protein L23 from Thermus thermophilus.'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The ribosomal protein L23 is a component of the large ribosomal subunit in | + | The ribosomal protein L23 is a component of the large ribosomal subunit in which it is located close to the peptide exit tunnel. In this position L23 plays a central role both for protein secretion and folding. We have determined the solution structure of L23 from Thermus thermophilus. Uncomplexed L23 consists of a well-ordered part, with four anti-parallel beta-strands and three alpha-helices connected as beta-alpha-beta-alpha-beta-beta-alpha, and a large and flexible loop inserted between the third and fourth beta-strand. The observed topology is distantly related to previously known structures, primarily within the area of RNA biochemistry. A comparison with RNA-complexed crystal structures of L23 from T. thermophilus, Deinococcus radiodurans and Haloarcula marismourtui, shows that the conformation of the well-ordered part is very similar in the uncomplexed and complexed states. However, the flexible loop found in the uncomplexed solution structure forms a rigid extended structure in the complexed crystal structures as it interacts with rRNA and becomes part of the exit tunnel wall. Structural characteristics of importance for the interaction with rRNA and with the ribosomal protein L29, as well as the functional role of L23, are discussed. |
==About this Structure== | ==About this Structure== | ||
| - | 1N88 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http:// | + | 1N88 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N88 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Thermus thermophilus]] | [[Category: Thermus thermophilus]] | ||
[[Category: Dontsova, M.]] | [[Category: Dontsova, M.]] | ||
| - | [[Category: Garber, M | + | [[Category: Garber, M B.]] |
[[Category: Hard, T.]] | [[Category: Hard, T.]] | ||
[[Category: Ohman, A.]] | [[Category: Ohman, A.]] | ||
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[[Category: translation]] | [[Category: translation]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:03:18 2008'' |
Revision as of 12:03, 21 February 2008
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NMR structure of the ribosomal protein L23 from Thermus thermophilus.
Overview
The ribosomal protein L23 is a component of the large ribosomal subunit in which it is located close to the peptide exit tunnel. In this position L23 plays a central role both for protein secretion and folding. We have determined the solution structure of L23 from Thermus thermophilus. Uncomplexed L23 consists of a well-ordered part, with four anti-parallel beta-strands and three alpha-helices connected as beta-alpha-beta-alpha-beta-beta-alpha, and a large and flexible loop inserted between the third and fourth beta-strand. The observed topology is distantly related to previously known structures, primarily within the area of RNA biochemistry. A comparison with RNA-complexed crystal structures of L23 from T. thermophilus, Deinococcus radiodurans and Haloarcula marismourtui, shows that the conformation of the well-ordered part is very similar in the uncomplexed and complexed states. However, the flexible loop found in the uncomplexed solution structure forms a rigid extended structure in the complexed crystal structures as it interacts with rRNA and becomes part of the exit tunnel wall. Structural characteristics of importance for the interaction with rRNA and with the ribosomal protein L29, as well as the functional role of L23, are discussed.
About this Structure
1N88 is a Single protein structure of sequence from Thermus thermophilus. Full crystallographic information is available from OCA.
Reference
NMR structure of the ribosomal protein L23 from Thermus thermophilus., Ohman A, Rak A, Dontsova M, Garber MB, Hard T, J Biomol NMR. 2003 Jun;26(2):131-7. PMID:12766408
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