1dwu: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
← Older edit
No edit summary
No edit summary
 
(14 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:1dwu.gif|left|200px]]


{{Structure
==Ribosomal protein L1==
|PDB= 1dwu |SIZE=350|CAPTION= <scene name='initialview01'>1dwu</scene>, resolution 2.8&Aring;
<StructureSection load='1dwu' size='340' side='right'caption='[[1dwu]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND=  
<table><tr><td colspan='2'>[[1dwu]] is a 2 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DWU FirstGlance]. <br>
|ACTIVITY=  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
|GENE= THE CORRESPONDING GENE IN E. COLI IS RPLA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2186 Methanothermococcus thermolithotrophicus])
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1dwu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dwu OCA], [https://pdbe.org/1dwu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dwu RCSB], [https://www.ebi.ac.uk/pdbsum/1dwu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dwu ProSAT]</span></td></tr>
|DOMAIN=
</table>
|RELATEDENTRY=
== Function ==
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dwu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dwu OCA], [http://www.ebi.ac.uk/pdbsum/1dwu PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1dwu RCSB]</span>
[https://www.uniprot.org/uniprot/RL1_METTL RL1_METTL] Probably involved in E site tRNA release (By similarity). Binds directly to 23S rRNA.  Protein L1 is also a translational repressor protein, it controls the translation of its operon by binding to its mRNA (By similarity).
}}
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dw/1dwu_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1dwu ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


'''RIBOSOMAL PROTEIN L1'''
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<ref>PMID:12037305</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1dwu" style="background-color:#fffaf0;"></div>


==Overview==
==See Also==
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.
*[[Ribosomal protein L1|Ribosomal protein L1]]
 
== References ==
==About this Structure==
<references/>
1DWU is a [[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].
__TOC__
 
</StructureSection>
==Reference==
[[Category: Large Structures]]
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:[http://www.ncbi.nlm.nih.gov/pubmed/12037305 12037305]
[[Category: Methanothermococcus thermolithotrophicus]]
[[Category: Methanothermococcus thermolithotrophicus]]
[[Category: Single protein]]
[[Category: Garber MB]]
[[Category: Garber, M B.]]
[[Category: Nevskaya NA]]
[[Category: Nevskaya, N A.]]
[[Category: Nikonov SV]]
[[Category: Nikonov, S V.]]
[[Category: Pavelyev MN]]
[[Category: Pavelyev, M N.]]
[[Category: Piendl W]]
[[Category: Piendl, W.]]
[[Category: Tishchenko SV]]
[[Category: Tishchenko, S V.]]
[[Category: protein synthesis]]
[[Category: ribosomal protein]]
[[Category: rna binding]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:50:25 2008''

Latest revision as of 11:08, 6 December 2023

Ribosomal protein L1Ribosomal protein L1

Structural highlights

1dwu is a 2 chain structure with sequence from Methanothermococcus thermolithotrophicus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.8Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

RL1_METTL Probably involved in E site tRNA release (By similarity). Binds directly to 23S rRNA. Protein L1 is also a translational repressor protein, it controls the translation of its operon by binding to its mRNA (By similarity).

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

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

1dwu, resolution 2.80Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
Retrieved from "https://proteopedia.openfox.io/wiki/index.php?title=1dwu&oldid=3976515"