1y39

From Proteopedia

(Difference between revisions)

Revision as of 16:23, 3 November 2021

Co-evolution of protein and RNA structures within a highly conserved ribosomal domain

Structural highlights

1y39 is a 4 chain structure with sequence from Atcc 12980. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , ,
NonStd Res:
Related:	1hc8
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[RL11_GEOSE] Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors.

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 X-ray crystal structure of a ribosomal L11-rRNA complex with chloroplast-like mutations in both protein and rRNA is presented. The global structure is almost identical to that of the wild-type (bacterial) complex, with only a small movement of the protein alpha helix away from the surface of the RNA required to accommodate the altered protein residue. In contrast, the specific hydrogen bonding pattern of the mutated residues is substantially different, and now includes a direct interaction between the protein side chain and an RNA base edge and a water-mediated contact. Comparison of the two structures allows the observations of sequence variation and relative affinities of wild-type and mutant complexes to be clearly rationalized, but reinforces the concept that there is no single simple code for protein-RNA recognition.

Coevolution of protein and RNA structures within a highly conserved ribosomal domain.,Dunstan MS, Guhathakurta D, Draper DE, Conn GL Chem Biol. 2005 Feb;12(2):201-6. PMID:15734647^[1]

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

References

↑ Dunstan MS, Guhathakurta D, Draper DE, Conn GL. Coevolution of protein and RNA structures within a highly conserved ribosomal domain. Chem Biol. 2005 Feb;12(2):201-6. PMID:15734647 doi:10.1016/j.chembiol.2004.11.019

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/1y39"

@@ Line 3: / Line 3: @@
 <StructureSection load='1y39' size='340' side='right'caption='[[1y39]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1y39]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_12980 Atcc 12980]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y39 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1Y39 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1y39]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_12980 Atcc 12980]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y39 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Y39 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=3CO:COBALT+(III)+ION'>3CO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3CO:COBALT+(III)+ION'>3CO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
 <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1hc8|1hc8]]</td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1hc8|1hc8]]</div></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=1y39 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y39 OCA], [http://pdbe.org/1y39 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1y39 RCSB], [http://www.ebi.ac.uk/pdbsum/1y39 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1y39 ProSAT]</span></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=1y39 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y39 OCA], [https://pdbe.org/1y39 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1y39 RCSB], [https://www.ebi.ac.uk/pdbsum/1y39 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1y39 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/RL11_GEOSE RL11_GEOSE]] Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors.
+[[https://www.uniprot.org/uniprot/RL11_GEOSE RL11_GEOSE]] Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1y39

From Proteopedia

Revision as of 16:23, 3 November 2021

Co-evolution of protein and RNA structures within a highly conserved ribosomal domain

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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