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1ily

From Proteopedia

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Current revision

Solution Structure of Ribosomal Protein L18 of Thermus thermophilus

Structural highlights

1ily is a 1 chain structure with sequence from Thermus thermophilus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

RL18_THETH This is one of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance (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

We have determined the solution structure of ribosomal protein L18 from Thermus thermophilus. L18 is a 12.5 kDa protein of the large subunit of the ribosome and binds to both 5 S and 23 S rRNA. In the uncomplexed state L18 folds to a mixed alpha/beta globular structure with a long disordered N-terminal region. We compared our high-resolution structure with RNA-complexed L18 from Haloarcula marismortui and T. thermophilus to examine RNA-induced as well as species-dependent structural differences. We also identified T. thermophilus S11 as a structural homologue and found that the structures of the RNA-recognition sites are conserved. Important features, for instance a bulge in the RNA-contacting beta-sheet, are conserved in both proteins. We suggest that the L18 fold recognizes a specific RNA motif and that the resulting RNA-protein-recognition module is tolerant to variations in sequence.

The solution structure of ribosomal protein L18 from Thermus thermophilus reveals a conserved RNA-binding fold.,Woestenenk EA, Gongadze GM, Shcherbakov DV, Rak AV, Garber MB, Hard T, Berglund H Biochem J. 2002 May 1;363(Pt 3):553-61. PMID:11964156^[1]

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

References

↑ Woestenenk EA, Gongadze GM, Shcherbakov DV, Rak AV, Garber MB, Hard T, Berglund H. The solution structure of ribosomal protein L18 from Thermus thermophilus reveals a conserved RNA-binding fold. Biochem J. 2002 May 1;363(Pt 3):553-61. PMID:11964156

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1ily"

@@ Line 1: / Line 1: @@
 ==Solution Structure of Ribosomal Protein L18 of Thermus thermophilus==
-<StructureSection load='1ily' size='340' side='right'caption='[[1ily]], [[NMR_Ensembles_of_Models | 27 NMR models]]' scene=''>
+<StructureSection load='1ily' size='340' side='right'caption='[[1ily]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1ily]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ILY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ILY FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1ily]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ILY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ILY FirstGlance]. <br>
-</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ily FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ily OCA], [http://pdbe.org/1ily PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ily RCSB], [http://www.ebi.ac.uk/pdbsum/1ily PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ily ProSAT]</span></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1ily FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ily OCA], [https://pdbe.org/1ily PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ily RCSB], [https://www.ebi.ac.uk/pdbsum/1ily PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ily ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/RL18_THETH RL18_THETH]] This is one of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance (By similarity).
+[https://www.uniprot.org/uniprot/RL18_THETH RL18_THETH] This is one of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance (By similarity).
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 35: / Line 36: @@
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Berglund, H]]
+[[Category: Thermus thermophilus]]
-[[Category: Garber, M B]]
+[[Category: Berglund H]]
-[[Category: Gongadze, G M]]
+[[Category: Garber MB]]
-[[Category: Hard, T]]
+[[Category: Gongadze GM]]
-[[Category: Rak, A V]]
+[[Category: Hard T]]
-[[Category: Shcherbakov, D V]]
+[[Category: Rak AV]]
-[[Category: Woestenenk, E A]]
+[[Category: Shcherbakov DV]]
-[[Category: Mixed alpha/beta]]
+[[Category: Woestenenk EA]]
-[[Category: Rna binding protein]]

1ily

From Proteopedia

Current revision

Solution Structure of Ribosomal Protein L18 of Thermus thermophilus

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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