|
|
| Line 3: |
Line 3: |
| | <StructureSection load='1bbu' size='340' side='right'caption='[[1bbu]], [[Resolution|resolution]] 2.70Å' scene=''> | | <StructureSection load='1bbu' size='340' side='right'caption='[[1bbu]], [[Resolution|resolution]] 2.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1bbu]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BBU OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1BBU FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1bbu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BBU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BBU FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LYS:LYSINE'>LYS</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]] 2.7Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">LYSS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LYS:LYSINE'>LYS</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Lysine--tRNA_ligase Lysine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.6 6.1.1.6] </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=1bbu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bbu OCA], [https://pdbe.org/1bbu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bbu RCSB], [https://www.ebi.ac.uk/pdbsum/1bbu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bbu ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1bbu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bbu OCA], [http://pdbe.org/1bbu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1bbu RCSB], [http://www.ebi.ac.uk/pdbsum/1bbu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1bbu ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/SYK1_ECOLI SYK1_ECOLI] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| Line 35: |
Line 36: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Ecoli]] | + | [[Category: Escherichia coli K-12]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lysine--tRNA ligase]]
| + | [[Category: Blanquet S]] |
| - | [[Category: Blanquet, S]] | + | [[Category: Brevet A]] |
| - | [[Category: Brevet, A]] | + | [[Category: Brick P]] |
| - | [[Category: Brick, P]] | + | [[Category: Chen J]] |
| - | [[Category: Chen, J]] | + | [[Category: Desogus G]] |
| - | [[Category: Desogus, G]] | + | [[Category: Onesti S]] |
| - | [[Category: Onesti, S]] | + | [[Category: Plateau P]] |
| - | [[Category: Plateau, P]] | + | |
| - | [[Category: Aminoacyl-trna synthetase]]
| + | |
| - | [[Category: Ligase]]
| + | |
| - | [[Category: Protein biosynthesis]]
| + | |
| Structural highlights
Function
SYK1_ECOLI
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
Lysyl-tRNA synthetase is a member of the class II aminoacyl-tRNA synthetases and catalyses the specific aminoacylation of tRNA(Lys). The crystal structure of the constitutive lysyl-tRNA synthetase (LysS) from Escherichia coli has been determined to 2.7 A resolution in the unliganded form and in a complex with the lysine substrate. A comparison between the unliganded and lysine-bound structures reveals major conformational changes upon lysine binding. The lysine substrate is involved in a network of hydrogen bonds. Two of these interactions, one between the alpha-amino group and the carbonyl oxygen of Gly 216 and the other between the carboxylate group and the side chain of Arg 262, trigger a subtle and complicated reorganization of the active site, involving the ordering of two loops (residues 215-217 and 444-455), a change in conformation of residues 393-409, and a rotation of a 4-helix bundle domain (located between motif 2 and 3) by 10 degrees. The result of these changes is a closing up of the active site upon lysine binding.
Structural studies of lysyl-tRNA synthetase: conformational changes induced by substrate binding.,Onesti S, Desogus G, Brevet A, Chen J, Plateau P, Blanquet S, Brick P Biochemistry. 2000 Oct 24;39(42):12853-61. PMID:11041850[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Onesti S, Desogus G, Brevet A, Chen J, Plateau P, Blanquet S, Brick P. Structural studies of lysyl-tRNA synthetase: conformational changes induced by substrate binding. Biochemistry. 2000 Oct 24;39(42):12853-61. PMID:11041850
|
