2vpl

From Proteopedia

(Difference between revisions)

Revision as of 10:48, 7 July 2021

The structure of the complex between the first domain of L1 protein from Thermus thermophilus and mRNA from Methanococcus jannaschii

Structural highlights

2vpl is a 4 chain structure with sequence from [1] and "flavobacterium_thermophilum"_yoshida_and_oshima_1971 "flavobacterium thermophilum" yoshida and oshima 1971. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	1zho, 1ad2, 2j01, 1eg0, 487d, 1u63
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[RL1_THETH] The L1 stalk is quite mobile in the ribosome, and is involved in E site tRNA release (By similarity). Binds directly to 23S rRNA.[HAMAP-Rule:MF_01318] Protein L1 is also a translational repressor protein, it controls the translation of the L11 operon by binding to its mRNA (By similarity).[HAMAP-Rule:MF_01318]

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 two-domain ribosomal protein L1 has a dual function as a primary rRNA-binding ribosomal protein and as a translational repressor that binds its own mRNA. Here, we report the crystal structure of a complex between the isolated domain I of L1 from the bacterium Thermus thermophilus and a specific mRNA fragment from Methanoccocus vannielii. In parallel, we report kinetic characteristics measured for complexes formed by intact TthL1 and its domain I with the specific mRNA fragment. Although, there is a close similarity between the RNA-protein contact regions in both complexes, the association rate constant is higher in the case of the complex formed by the isolated domain I. This finding demonstrates that domain II hinders mRNA recognition by the intact TthL1.

Domain II of Thermus thermophilus ribosomal protein L1 hinders recognition of its mRNA.,Tishchenko S, Kljashtorny V, Kostareva O, Nevskaya N, Nikulin A, Gulak P, Piendl W, Garber M, Nikonov S J Mol Biol. 2008 Nov 7;383(2):301-5. Epub 2008 Aug 29. PMID:18778715^[1]

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

References

↑ Tishchenko S, Kljashtorny V, Kostareva O, Nevskaya N, Nikulin A, Gulak P, Piendl W, Garber M, Nikonov S. Domain II of Thermus thermophilus ribosomal protein L1 hinders recognition of its mRNA. J Mol Biol. 2008 Nov 7;383(2):301-5. Epub 2008 Aug 29. PMID:18778715 doi:10.1016/j.jmb.2008.08.058

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/2vpl"

@@ Line 3: / Line 3: @@
 <StructureSection load='2vpl' size='340' side='right'caption='[[2vpl]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2vpl]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/ ] and [http://en.wikipedia.org/wiki/"flavobacterium_thermophilum"_yoshida_and_oshima_1971 "flavobacterium thermophilum" yoshida and oshima 1971]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VPL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VPL FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2vpl]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/ ] and [https://en.wikipedia.org/wiki/"flavobacterium_thermophilum"_yoshida_and_oshima_1971 "flavobacterium thermophilum" yoshida and oshima 1971]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VPL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VPL FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1zho|1zho]], [[1ad2|1ad2]], [[2j01|2j01]], [[1eg0|1eg0]], [[487d|487d]], [[1u63|1u63]]</td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1zho|1zho]], [[1ad2|1ad2]], [[2j01|2j01]], [[1eg0|1eg0]], [[487d|487d]], [[1u63|1u63]]</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=2vpl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vpl OCA], [http://pdbe.org/2vpl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2vpl RCSB], [http://www.ebi.ac.uk/pdbsum/2vpl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2vpl 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=2vpl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vpl OCA], [https://pdbe.org/2vpl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vpl RCSB], [https://www.ebi.ac.uk/pdbsum/2vpl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vpl ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/RL1_THETH RL1_THETH]] The L1 stalk is quite mobile in the ribosome, and is involved in E site tRNA release (By similarity). Binds directly to 23S rRNA.[HAMAP-Rule:MF_01318]  Protein L1 is also a translational repressor protein, it controls the translation of the L11 operon by binding to its mRNA (By similarity).[HAMAP-Rule:MF_01318]
+[[https://www.uniprot.org/uniprot/RL1_THETH RL1_THETH]] The L1 stalk is quite mobile in the ribosome, and is involved in E site tRNA release (By similarity). Binds directly to 23S rRNA.[HAMAP-Rule:MF_01318]  Protein L1 is also a translational repressor protein, it controls the translation of the L11 operon by binding to its mRNA (By similarity).[HAMAP-Rule:MF_01318]
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

2vpl

From Proteopedia

Revision as of 10:48, 7 July 2021

The structure of the complex between the first domain of L1 protein from Thermus thermophilus and mRNA from Methanococcus jannaschii

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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