1DWU

Ribosomal protein L1

Summary for 1DWU

• Entry DOI: 10.2210/pdb1dwu/pdb
• Related: 1CJS
• Descriptor: RIBOSOMAL PROTEIN L1 (1 entity in total)
• Functional Keywords: ribosomal protein, rna binding, protein synthesis
• Biological source: METHANOCOCCUS THERMOLITHOTROPHICUS
• Total number of polymer chains: 2
• Total formula weight: 47663.75

Authors

Tishchenko, S.V.,Nevskaya, N.A.,Pavelyev, M.N.,Nikonov, S.V.,Garber, M.B.,Piendl, W. (deposition date: 1999-12-13, release date: 2000-12-07, Last modification date: 2023-12-06)

Primary citation

Nevskaya, N.A.,Tishchenko, S.V.,Paveliev, M.,Smolinskaya, Y.,Fedorov, R.,Piendl, W.,Nakamura, Y.,Toyoda, T.,Garber, M.B.,Nikonov, S.V.
Structure of Ribosomal Protein L1 from Methanococcus Thermolithotrophicus. Functionally Important Structural Invariants on the L1 Surface
Acta Crystallogr.,Sect.D, 58:1023-, 2002

PubMed Abstract: The crystal structure of ribosomal protein L1 from the archaeon Methanococcus thermolithotrophicus has been determined at 2.7 A resolution. The crystals belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 67.0, b = 70.1, c = 106.3 A and two molecules per asymmetric unit. The structure was solved by the molecular-replacement method with AMoRe and refined with CNS to an R value of 18.9% and an R(free) of 25.4% in the resolution range 30-2.7 A. Comparison of this structure with those obtained previously for two L1 proteins from other sources (the bacterium Thermus thermophilus and the archaeon M. jannaschii) as well as detailed analysis of intermolecular contacts in the corresponding L1 crystals reveal structural invariants on the molecular surface which are probably important for binding the 23S ribosomal RNA and protein function within the ribosome.

PubMed: 12037305
DOI: 10.1107/S0907444902006157

Experimental method

X-RAY DIFFRACTION (2.8 Å)