1n88
From Proteopedia
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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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