1dwu: Difference between revisions

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New page: left|200px<br /><applet load="1dwu" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dwu, resolution 2.8Å" /> '''RIBOSOMAL PROTEIN L1'...
 
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[[Image:1dwu.gif|left|200px]]<br /><applet load="1dwu" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1dwu.gif|left|200px]]<br /><applet load="1dwu" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1dwu, resolution 2.8&Aring;" />
caption="1dwu, resolution 2.8&Aring;" />
'''RIBOSOMAL PROTEIN L1'''<br />
'''RIBOSOMAL PROTEIN L1'''<br />


==Overview==
==Overview==
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.
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.


==About this Structure==
==About this Structure==
1DWU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methanothermococcus_thermolithotrophicus Methanothermococcus thermolithotrophicus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DWU OCA].  
1DWU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methanothermococcus_thermolithotrophicus Methanothermococcus thermolithotrophicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DWU OCA].  


==Reference==
==Reference==
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[[Category: Methanothermococcus thermolithotrophicus]]
[[Category: Methanothermococcus thermolithotrophicus]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Garber, M.B.]]
[[Category: Garber, M B.]]
[[Category: Nevskaya, N.A.]]
[[Category: Nevskaya, N A.]]
[[Category: Nikonov, S.V.]]
[[Category: Nikonov, S V.]]
[[Category: Pavelyev, M.N.]]
[[Category: Pavelyev, M N.]]
[[Category: Piendl, W.]]
[[Category: Piendl, W.]]
[[Category: Tishchenko, S.V.]]
[[Category: Tishchenko, S V.]]
[[Category: protein synthesis]]
[[Category: protein synthesis]]
[[Category: ribosomal protein]]
[[Category: ribosomal protein]]
[[Category: rna binding]]
[[Category: rna binding]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:38:46 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:21:21 2008''

Revision as of 13:21, 21 February 2008

File:1dwu.gif


1dwu, resolution 2.8Å

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RIBOSOMAL PROTEIN L1

OverviewOverview

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.

About this StructureAbout this Structure

1DWU is a Single protein structure of sequence from Methanothermococcus thermolithotrophicus. Full crystallographic information is available from OCA.

ReferenceReference

Structure of ribosomal protein L1 from Methanococcus thermolithotrophicus. Functionally important structural invariants on the L1 surface., Nevskaya N, Tishchenko S, Paveliev M, Smolinskaya Y, Fedorov R, Piendl W, Nakamura Y, Toyoda T, Garber M, Nikonov S, Acta Crystallogr D Biol Crystallogr. 2002 Jun;58(Pt 6 Pt 2):1023-9. Epub, 2002 May 29. PMID:12037305

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