4a91

From Proteopedia

(Difference between revisions)

Current revision

Crystal structure of the glutamyl-queuosine tRNAAsp synthetase from E. coli complexed with L-glutamate

Structural highlights

4a91 is a 1 chain structure with sequence from Escherichia coli. This structure supersedes the now removed PDB entry 2zlz. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.75Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

GLUQ_ECOLI Catalyzes the tRNA-independent activation of glutamate in presence of ATP and the subsequent transfer of glutamate onto tRNA(Asp). Glutamate is transferred on the 2-amino-5-(4,5-dihydroxy-2-cyclopenten-1-yl) moiety of the queuosine in position 34 of the tRNA(Asp), the wobble position of the QUC anticodon. Does not transfer glutamate to either tRNA(Glu) or tRNA(Gln). The incapacity of the glutamylated tRNA(Asp) to bind elongation factor Tu suggests that it is not involved in ribosomal protein biosynthesis.^[1] ^[2] ^[3]

Publication Abstract from PubMed

Glutamyl-queuosine tRNA(Asp) synthetase (Glu-Q-RS) from Escherichia coli is a paralog of the catalytic core of glutamyl-tRNA synthetase (GluRS) that catalyzes glutamylation of queuosine in the wobble position of tRNA(Asp). Despite important structural similarities, Glu-Q-RS and GluRS diverge strongly by their functional properties. The only feature common to both enzymes consists in the activation of Glu to form Glu-AMP, the intermediate of transfer RNA (tRNA) aminoacylation. However, both enzymes differ by the mechanism of selection of the cognate amino acid and by the mechanism of its activation. Whereas GluRS selects l-Glu and activates it only in the presence of the cognate tRNA(Glu), Glu-Q-RS forms Glu-AMP in the absence of tRNA. Moreover, while GluRS transfers the activated Glu to the 3' accepting end of the cognate tRNA(Glu), Glu-Q-RS transfers the activated Glu to Q34 located in the anticodon loop of the noncognate tRNA(Asp). In order to gain insight into the structural elements leading to distinct mechanisms of amino acid activation, we solved the three-dimensional structure of Glu-Q-RS complexed to Glu and compared it to the structure of the GluRS.Glu complex. Comparison of the catalytic site of Glu-Q-RS with that of GluRS, combined with binding experiments of amino acids, shows that a restricted number of residues determine distinct catalytic properties of amino acid recognition and activation by the two enzymes. Furthermore, to explore the structural basis of the distinct aminoacylation properties of the two enzymes and to understand why Glu-Q-RS glutamylates only tRNA(Asp) among the tRNAs possessing queuosine in position 34, we performed a tRNA mutational analysis to search for the elements of tRNA(Asp) that determine recognition by Glu-Q-RS. The analyses made on tRNA(Asp) and tRNA(Asn) show that the presence of a C in position 38 is crucial for glutamylation of Q34. The results are discussed in the context of the evolution and adaptation of the tRNA glutamylation system.

Crystal structure of glutamyl-queuosine tRNAAsp synthetase complexed with L-glutamate: structural elements mediating tRNA-independent activation of glutamate and glutamylation of tRNAAsp anticodon.,Blaise M, Olieric V, Sauter C, Lorber B, Roy B, Karmakar S, Banerjee R, Becker HD, Kern D J Mol Biol. 2008 Sep 19;381(5):1224-37. Epub 2008 Jun 26. PMID:18602926^[4]

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

References

↑ Dubois DY, Blaise M, Becker HD, Campanacci V, Keith G, Giege R, Cambillau C, Lapointe J, Kern D. An aminoacyl-tRNA synthetase-like protein encoded by the Escherichia coli yadB gene glutamylates specifically tRNAAsp. Proc Natl Acad Sci U S A. 2004 May 18;101(20):7530-5. Epub 2004 Apr 19. PMID:15096594 doi:http://dx.doi.org/10.1073/pnas.0401634101
↑ Salazar JC, Ambrogelly A, Crain PF, McCloskey JA, Soll D. A truncated aminoacyl-tRNA synthetase modifies RNA. Proc Natl Acad Sci U S A. 2004 May 18;101(20):7536-41. Epub 2004 Apr 19. PMID:15096612 doi:http://dx.doi.org/10.1073/pnas.0401982101
↑ Blaise M, Becker HD, Keith G, Cambillau C, Lapointe J, Giege R, Kern D. A minimalist glutamyl-tRNA synthetase dedicated to aminoacylation of the tRNAAsp QUC anticodon. Nucleic Acids Res. 2004 May 18;32(9):2768-75. Print 2004. PMID:15150343 doi:http://dx.doi.org/10.1093/nar/gkh608
↑ Blaise M, Olieric V, Sauter C, Lorber B, Roy B, Karmakar S, Banerjee R, Becker HD, Kern D. Crystal structure of glutamyl-queuosine tRNAAsp synthetase complexed with L-glutamate: structural elements mediating tRNA-independent activation of glutamate and glutamylation of tRNAAsp anticodon. J Mol Biol. 2008 Sep 19;381(5):1224-37. Epub 2008 Jun 26. PMID:18602926 doi:10.1016/j.jmb.2008.06.053

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4a91"

@@ Line 1: / Line 1: @@
 ==Crystal structure of the glutamyl-queuosine tRNAAsp synthetase from E. coli complexed with L-glutamate==
-<StructureSection load='4a91' size='340' side='right' caption='[[4a91]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
+<StructureSection load='4a91' size='340' side='right'caption='[[4a91]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4a91]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2zlz 2zlz]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4A91 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4A91 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4a91]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2zlz 2zlz]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4A91 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4A91 FirstGlance]. <br>
-</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GLU:GLUTAMIC+ACID'>GLU</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene><br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.75&#8491;</td></tr>
-<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4a91 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a91 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4a91 RCSB], [http://www.ebi.ac.uk/pdbsum/4a91 PDBsum]</span></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLU:GLUTAMIC+ACID'>GLU</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-<table>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4a91 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a91 OCA], [https://pdbe.org/4a91 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4a91 RCSB], [https://www.ebi.ac.uk/pdbsum/4a91 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4a91 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/GLUQ_ECOLI GLUQ_ECOLI] Catalyzes the tRNA-independent activation of glutamate in presence of ATP and the subsequent transfer of glutamate onto tRNA(Asp). Glutamate is transferred on the 2-amino-5-(4,5-dihydroxy-2-cyclopenten-1-yl) moiety of the queuosine in position 34 of the tRNA(Asp), the wobble position of the QUC anticodon. Does not transfer glutamate to either tRNA(Glu) or tRNA(Gln). The incapacity of the glutamylated tRNA(Asp) to bind elongation factor Tu suggests that it is not involved in ribosomal protein biosynthesis.<ref>PMID:15096594</ref> <ref>PMID:15096612</ref> <ref>PMID:15150343</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 12: / Line 16: @@
 Crystal structure of glutamyl-queuosine tRNAAsp synthetase complexed with L-glutamate: structural elements mediating tRNA-independent activation of glutamate and glutamylation of tRNAAsp anticodon.,Blaise M, Olieric V, Sauter C, Lorber B, Roy B, Karmakar S, Banerjee R, Becker HD, Kern D J Mol Biol. 2008 Sep 19;381(5):1224-37. Epub 2008 Jun 26. PMID:18602926<ref>PMID:18602926</ref>
-From MEDLINEÂ®/PubMedÂ®, a database of the U.S. National Library of Medicine.<br>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4a91" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Aminoacyl tRNA synthetase 3D structures|Aminoacyl tRNA synthetase 3D structures]]
 == References ==
 <references/>
@@ Line 19: / Line 27: @@
 </StructureSection>
 [[Category: Escherichia coli]]
-[[Category: Banerjee, R.]]
+[[Category: Large Structures]]
-[[Category: Becker, H D.]]
+[[Category: Banerjee R]]
-[[Category: Blaise, M.]]
+[[Category: Becker HD]]
-[[Category: Karmakar, S.]]
+[[Category: Blaise M]]
-[[Category: Kern, D.]]
+[[Category: Karmakar S]]
-[[Category: Lorber, B.]]
+[[Category: Kern D]]
-[[Category: Olieric, V.]]
+[[Category: Lorber B]]
-[[Category: Roy, B.]]
+[[Category: Olieric V]]
-[[Category: Sauter, C.]]
+[[Category: Roy B]]
-[[Category: Ligase]]
+[[Category: Sauter C]]

4a91

From Proteopedia

Current revision

Crystal structure of the glutamyl-queuosine tRNAAsp synthetase from E. coli complexed with L-glutamate

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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