Online ordering is currently unavailable due to technical issues. We apologise for any delays responding to customers while we resolve this. For further updates please visit our website: https://www.cambridge.org/news-and-insights/technical-incident
We use cookies to distinguish you from other users and to provide you with a better experience on our websites. Close this message to accept cookies or find out how to manage your cookie settings.
To save content items to your account,
please confirm that you agree to abide by our usage policies.
If this is the first time you use this feature, you will be asked to authorise Cambridge Core to connect with your account.
Find out more about saving content to .
To save content items to your Kindle, first ensure coreplatform@cambridge.org
is added to your Approved Personal Document E-mail List under your Personal Document Settings
on the Manage Your Content and Devices page of your Amazon account. Then enter the ‘name’ part
of your Kindle email address below.
Find out more about saving to your Kindle.
Note you can select to save to either the @free.kindle.com or @kindle.com variations.
‘@free.kindle.com’ emails are free but can only be saved to your device when it is connected to wi-fi.
‘@kindle.com’ emails can be delivered even when you are not connected to wi-fi, but note that service fees apply.
Ribosomal protein L5 is a 5S rRNA binding protein in
the large subunit and plays an essential role in the promotion
of a particular conformation of 5S rRNA. The crystal structure
of the ribosomal protein L5 from Bacillus stearothermophilus
has been determined at 1.8 Å resolution. The molecule
consists of a five-stranded antiparallel β-sheet and
four α-helices, which fold in a way that is topologically
similar to the ribonucleoprotein (RNP) domain. The molecular
shape and electrostatic representation suggest that the
concave surface and loop regions are involved in 5S rRNA
binding. To identify amino acid residues responsible for
5S rRNA binding, we made use of Ala-scanning mutagenesis
of evolutionarily conserved amino acids occurring in the
β-strands and loop regions. The mutations of Asn37
at the β1-strand and Gln63 at the loop between helix
2 and β3-strand as well as that of Phe77 at the tip
of the loop structure between the β2- and β3-strands
caused a significant reduction in 5S rRNA binding. In addition,
the mutations of Thr90 on the β3-strand and Ile141
and Asp144 at the loop between β4- and β5-strands
moderately reduced the 5S rRNA-binding affinity. Comparison
of these results with the more recently analyzed structure
of the 50S subunit from Haloarcula marismortui
suggests that there are significant differences in the
structure at N- and C-terminal regions and probably in
the 5S rRNA binding.
Recommend this
Email your librarian or administrator to recommend adding this to your organisation's collection.