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1x54

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Current revision

Crystal structure of asparaginyl-tRNA synthetase from Pyrococcus horikoshii complexed with asparaginyl-adenylate

Structural highlights

1x54 is a 1 chain structure with sequence from Pyrococcus horikoshii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.45Å
Ligands:	, ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN

Function

SYN_PYRHO

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

Asparaginyl-tRNA synthetase (AsnRS) is a member of the class-II aminoacyl-tRNA synthetases, and is responsible for catalyzing the specific aminoacylation of tRNA(Asn) with asparagine. Here, the crystal structure of AsnRS from Pyrococcus horikoshii, complexed with asparaginyl-adenylate (Asn-AMP), was determined at 1.45 A resolution, and those of free AsnRS and AsnRS complexed with an Asn-AMP analog (Asn-SA) were solved at 1.98 and 1.80 A resolutions, respectively. All of the crystal structures have many solvent molecules, which form a network of hydrogen-bonding interactions that surrounds the entire AsnRS molecule. In the AsnRS/Asn-AMP complex (or the AsnRS/Asn-SA), one side of the bound Asn-AMP (or Asn-SA) is completely covered by the solvent molecules, which complement the binding site. In particular, two of these water molecules were found to interact directly with the asparagine amide and carbonyl groups, respectively, and to contribute to the formation of a pocket highly complementary to the asparagine side-chain. Thus, these two water molecules appear to play a key role in the strict recognition of asparagine and the discrimination against aspartic acid by the AsnRS. This water-assisted asparagine recognition by the AsnRS strikingly contrasts with the fact that the aspartic acid recognition by the closely related aspartyl-tRNA synthetase is achieved exclusively through extensive interactions with protein amino acid residues. Furthermore, based on a docking model of AsnRS and tRNA, a single arginine residue (Arg83) in the AsnRS was postulated to be involved in the recognition of the third position of the tRNA(Asn) anticodon (U36). We performed a mutational analysis of this particular arginine residue, and confirmed its significance in the tRNA recognition.

Structural basis of the water-assisted asparagine recognition by asparaginyl-tRNA synthetase.,Iwasaki W, Sekine S, Kuroishi C, Kuramitsu S, Shirouzu M, Yokoyama S J Mol Biol. 2006 Jul 7;360(2):329-42. Epub 2006 May 15. PMID:16753178^[1]

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

References

↑ Iwasaki W, Sekine S, Kuroishi C, Kuramitsu S, Shirouzu M, Yokoyama S. Structural basis of the water-assisted asparagine recognition by asparaginyl-tRNA synthetase. J Mol Biol. 2006 Jul 7;360(2):329-42. Epub 2006 May 15. PMID:16753178 doi:10.1016/j.jmb.2006.04.068

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/1x54"

Categories: Large Structures | Pyrococcus horikoshii | Iwasaki W | Sekine S | Yokoyama S

@@ Line 3: / Line 3: @@
 <StructureSection load='1x54' size='340' side='right'caption='[[1x54]], [[Resolution|resolution]] 1.45&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1x54]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/'pyrococcus_shinkaii' 'pyrococcus shinkaii']. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1X54 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1X54 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1x54]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_horikoshii Pyrococcus horikoshii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1X54 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1X54 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=4AD:4-AMINO-1,4-DIOXOBUTAN-2-AMINIUM+ADENOSINE-5-MONOPHOSPHATE'>4AD</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.45&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1x55|1x55]], [[1x56|1x56]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=4AD:4-AMINO-1,4-DIOXOBUTAN-2-AMINIUM+ADENOSINE-5-MONOPHOSPHATE'>4AD</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Asparagine--tRNA_ligase Asparagine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.22 6.1.1.22] </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=1x54 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1x54 OCA], [https://pdbe.org/1x54 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1x54 RCSB], [https://www.ebi.ac.uk/pdbsum/1x54 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1x54 ProSAT], [https://www.topsan.org/Proteins/RSGI/1x54 TOPSAN]</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=1x54 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1x54 OCA], [http://pdbe.org/1x54 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1x54 RCSB], [http://www.ebi.ac.uk/pdbsum/1x54 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1x54 ProSAT], [http://www.topsan.org/Proteins/RSGI/1x54 TOPSAN]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/SYN_PYRHO SYN_PYRHO]
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 35: / Line 36: @@
 __TOC__
 </StructureSection>
-[[Category: Pyrococcus shinkaii]]
-[[Category: Asparagine--tRNA ligase]]
 [[Category: Large Structures]]
-[[Category: Iwasaki, W]]
+[[Category: Pyrococcus horikoshii]]
-[[Category: Structural genomic]]
+[[Category: Iwasaki W]]
-[[Category: Sekine, S]]
+[[Category: Sekine S]]
-[[Category: Yokoyama, S]]
+[[Category: Yokoyama S]]
-[[Category: Aminoacyl-trna synthetase]]
-[[Category: Ligase]]
-[[Category: Rsgi]]

1x54

From Proteopedia

Current revision

Crystal structure of asparaginyl-tRNA synthetase from Pyrococcus horikoshii complexed with asparaginyl-adenylate

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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