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1kog

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Revision as of 07:17, 11 October 2017

Crystal structure of E. coli threonyl-tRNA synthetase interacting with the essential domain of its mRNA operator

Structural highlights

1kog is a 16 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	1evl, 1qf6
Activity:	Threonine--tRNA ligase, with EC number 6.1.1.3
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[SYT_ECOLI] ThrS is also a translational repressor protein, it controls the translation of its own gene by binding to its mRNA.[HAMAP-Rule:MF_00184]

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

Escherichia coli threonyl-tRNA synthetase (ThrRS) represses the translation of its own messenger RNA by binding to an operator located upstream of the initiation codon. The crystal structure of the complex between the core of ThrRS and the essential domain of the operator shows that the mRNA uses the recognition mode of the tRNA anticodon loop to initiate binding. The final positioning of the operator, upon which the control mechanism is based, relies on a characteristic RNA motif adapted to the enzyme surface. The finding of other thrS operators that have this conserved motif leads to a generalization of this regulatory mechanism to a subset of Gram-negative bacteria.

Structural basis of translational control by Escherichia coli threonyl tRNA synthetase.,Torres-Larios A, Dock-Bregeon AC, Romby P, Rees B, Sankaranarayanan R, Caillet J, Springer M, Ehresmann C, Ehresmann B, Moras D Nat Struct Biol. 2002 May;9(5):343-7. PMID:11953757^[1]

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

References

↑ Torres-Larios A, Dock-Bregeon AC, Romby P, Rees B, Sankaranarayanan R, Caillet J, Springer M, Ehresmann C, Ehresmann B, Moras D. Structural basis of translational control by Escherichia coli threonyl tRNA synthetase. Nat Struct Biol. 2002 May;9(5):343-7. PMID:11953757 doi:10.1038/nsb789

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

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

@@ Line 1: / Line 1: @@
 ==Crystal structure of E. coli threonyl-tRNA synthetase interacting with the essential domain of its mRNA operator==
 <StructureSection load='1kog' size='340' side='right' caption='[[1kog]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1evl|1evl]], [[1qf6|1qf6]]</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Threonine--tRNA_ligase Threonine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.3 6.1.1.3] </span></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=1kog FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kog OCA], [http://pdbe.org/1kog PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1kog RCSB], [http://www.ebi.ac.uk/pdbsum/1kog PDBsum]</span></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=1kog FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kog OCA], [http://pdbe.org/1kog PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1kog RCSB], [http://www.ebi.ac.uk/pdbsum/1kog PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1kog ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 18: / Line 19: @@
     <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/chain_selection.php?pdb_ID=2ata 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=1kog ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 29: / Line 30: @@
 </div>
 <div class="pdbe-citations 1kog" style="background-color:#fffaf0;"></div>
-==See Also==
-*[[Aminoacyl tRNA Synthetase|Aminoacyl tRNA Synthetase]]
 == References ==
 <references/>

1kog

From Proteopedia

Revision as of 07:17, 11 October 2017

Crystal structure of E. coli threonyl-tRNA synthetase interacting with the essential domain of its mRNA operator

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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