4F9T

Ribosomal protein L1 from Thermus thermophilus with substitution Thr217Ala

Summary for 4F9T

• Entry DOI: 10.2210/pdb4f9t/pdb
• Related: 1AD2 1I2A 1MZP 1U63 1ZHO 2HW8 2OUM 2OV7 2VPL
• Descriptor: 50S ribosomal protein L1, (4S)-2-METHYL-2,4-PENTANEDIOL, (4R)-2-METHYLPENTANE-2,4-DIOL, ... (5 entities in total)
• Functional Keywords: rossmann fold, ribosomal protein, rna
• Biological source: Thermus thermophilus
• Total number of polymer chains: 1
• Total formula weight: 26271.00

Authors

Kljashtorny, V.G.,Volchkov, S.A.,Nikonova, E.Y.,Kostareva, O.S.,Tishchenko, S.V.,Nevskaya, N.A.,Nikonov, S.V. (deposition date: 2012-05-21, release date: 2012-08-08, Last modification date: 2024-02-28)

Primary citation

Nikonova, E.I.u.,Volchkov, S.A.,Kliashtornyi, V.G.,Tishchenko, S.V.,Kostareva, O.S.,Nevskaia, N.A.,Nikonov, O.S.,Gabdulkhakov, A.G.,Nikulin, A.D.,Davydova, N.L.,Strel'tsov, V.A.,Garber, M.B.,Nikonov, S.V.
[Crystal structures of mutant ribosomal proteins L1].
MOL.BIOL.(MOSCOW), 41:688-696, 2007

PubMed Abstract: Nine mutant forms of ribosomal proteins L1 from the bacterium Thermus thermophilus and the archaeon Methanococcus jannaschii were obtained. Their crystal structures were determined and analyzed. Earlier determined structure of S179C TthL1 was also thoroughly analyzed. Five from ten mutant proteins reveal essential changes of spatial structure caused by surface point mutation. It proves that for correct studies of biological processes by site-directed mutagenesis it is necessary to determine or at least to model spatial structures of mutant proteins. Detailed comparison of mutant L1 structures with that of corresponding wild type proteins reveals that side chain of a mutated amino acid residue tries to locate like the side chain of the original residue in the wild type protein. This observation helps to model the mutant structures.

PubMed: 17936990

Experimental method

X-RAY DIFFRACTION (1.46 Å)