1dd3: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1dd3]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DD3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DD3 FirstGlance]. <br>
<table><tr><td colspan='2'>[[1dd3]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DD3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DD3 FirstGlance]. <br>
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1dd3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dd3 OCA], [https://pdbe.org/1dd3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dd3 RCSB], [https://www.ebi.ac.uk/pdbsum/1dd3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dd3 ProSAT]</span></td></tr>
</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&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1dd3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dd3 OCA], [https://pdbe.org/1dd3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dd3 RCSB], [https://www.ebi.ac.uk/pdbsum/1dd3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dd3 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/RL7_THEMA RL7_THEMA]] Seems to be the binding site for several of the factors involved in protein synthesis and appears to be essential for accurate translation.  
[https://www.uniprot.org/uniprot/RL7_THEMA RL7_THEMA] Seems to be the binding site for several of the factors involved in protein synthesis and appears to be essential for accurate translation.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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=1dd3 ConSurf].
</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=1dd3 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Protein L12, the only multicopy component of the ribosome, is presumed to be involved in the binding of translation factors, stimulating factor-dependent GTP hydrolysis. Crystal structures of L12 from Thermotogamaritima have been solved in two space groups by the multiple anomalous dispersion method and refined at 2.4 and 2.0 A resolution. In both crystal forms, an asymmetric unit comprises two full-length L12 molecules and two N-terminal L12 fragments that are associated in a specific, hetero-tetrameric complex with one non-crystallographic 2-fold axis. The two full-length proteins form a tight, symmetric, parallel dimer, mainly through their N-terminal domains. Each monomer of this central dimer additionally associates in a different way with an N-terminal L12 fragment. Both dimerization modes are unlike models proposed previously and suggest that similar complexes may occur in vivo and in situ. The structures also display different L12 monomer conformations, in accord with the suggested dynamic role of the protein in the ribosomal translocation process. The structures have been submitted to the Protein Databank (http://www.rcsb.org/pdb) under accession numbers 1DD3 and 1DD4.
Flexibility, conformational diversity and two dimerization modes in complexes of ribosomal protein L12.,Wahl MC, Bourenkov GP, Bartunik HD, Huber R EMBO J. 2000 Jan 17;19(2):174-86. PMID:10637222<ref>PMID:10637222</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1dd3" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Ribosomal protein L7/L12|Ribosomal protein L7/L12]]
*[[Ribosomal protein L7/L12|Ribosomal protein L7/L12]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Thermotoga maritima]]
[[Category: Thermotoga maritima]]
[[Category: Bartunik, H D]]
[[Category: Bartunik HD]]
[[Category: Bourenkov, G P]]
[[Category: Bourenkov GP]]
[[Category: Huber, R]]
[[Category: Huber R]]
[[Category: Wahl, M C]]
[[Category: Wahl MC]]
[[Category: Alpha-beta structure]]
[[Category: Dimer formation]]
[[Category: Domain]]
[[Category: Five-helix- bundle]]
[[Category: Flexibility]]
[[Category: Four-helix-bundle]]
[[Category: Helical hairpin]]
[[Category: Hinge region]]
[[Category: Ribosome]]

Latest revision as of 09:52, 7 February 2024

CRYSTAL STRUCTURE OF RIBOSOMAL PROTEIN L12 FROM THERMOTOGA MARITIMACRYSTAL STRUCTURE OF RIBOSOMAL PROTEIN L12 FROM THERMOTOGA MARITIMA

Structural highlights

1dd3 is a 4 chain structure with sequence from Thermotoga maritima. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

RL7_THEMA Seems to be the binding site for several of the factors involved in protein synthesis and appears to be essential for accurate translation.

Evolutionary Conservation

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

See Also

1dd3, resolution 2.00Å

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