1iq4
From Proteopedia
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| - | [[Image:1iq4.jpg|left|200px]] | + | [[Image:1iq4.jpg|left|200px]] |
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| - | '''5S-RRNA BINDING RIBOSOMAL PROTEIN L5 FROM BACILLUS STEAROTHERMOPHILUS''' | + | {{Structure |
| + | |PDB= 1iq4 |SIZE=350|CAPTION= <scene name='initialview01'>1iq4</scene>, resolution 1.8Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''5S-RRNA BINDING RIBOSOMAL PROTEIN L5 FROM BACILLUS STEAROTHERMOPHILUS''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1IQ4 is a [ | + | 1IQ4 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IQ4 OCA]. |
==Reference== | ==Reference== | ||
| - | Ribosomal protein L5 has a highly twisted concave surface and flexible arms responsible for rRNA binding., Nakashima T, Yao M, Kawamura S, Iwasaki K, Kimura M, Tanaka I, RNA. 2001 May;7(5):692-701. PMID:[http:// | + | Ribosomal protein L5 has a highly twisted concave surface and flexible arms responsible for rRNA binding., Nakashima T, Yao M, Kawamura S, Iwasaki K, Kimura M, Tanaka I, RNA. 2001 May;7(5):692-701. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11350033 11350033] |
[[Category: Geobacillus stearothermophilus]] | [[Category: Geobacillus stearothermophilus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: rrna-binding]] | [[Category: rrna-binding]] | ||
| - | ''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 11:53:28 2008'' |
Revision as of 09:53, 20 March 2008
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5S-RRNA BINDING RIBOSOMAL PROTEIN L5 FROM BACILLUS STEAROTHERMOPHILUS
Overview
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 A resolution. The molecule consists of a five-stranded antiparallel beta-sheet and four alpha-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 beta-strands and loop regions. The mutations of Asn37 at the beta1-strand and Gln63 at the loop between helix 2 and beta3-strand as well as that of Phe77 at the tip of the loop structure between the beta2- and beta3-strands caused a significant reduction in 5S rRNA binding. In addition, the mutations of Thr90 on the beta3-strand and Ile141 and Asp144 at the loop between beta4- and beta5-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.
About this Structure
1IQ4 is a Single protein structure of sequence from Geobacillus stearothermophilus. Full crystallographic information is available from OCA.
Reference
Ribosomal protein L5 has a highly twisted concave surface and flexible arms responsible for rRNA binding., Nakashima T, Yao M, Kawamura S, Iwasaki K, Kimura M, Tanaka I, RNA. 2001 May;7(5):692-701. PMID:11350033
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