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- | [[Image:2ip1.gif|left|200px]] | |
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- | {{Structure
| + | ==Crystal Structure Analysis of S. cerevisiae Tryptophanyl tRNA Synthetase== |
- | |PDB= 2ip1 |SIZE=350|CAPTION= <scene name='initialview01'>2ip1</scene>, resolution 1.80Å
| + | <StructureSection load='2ip1' size='340' side='right'caption='[[2ip1]], [[Resolution|resolution]] 1.80Å' scene=''> |
- | |SITE=
| + | == Structural highlights == |
- | |LIGAND= <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>
| + | <table><tr><td colspan='2'>[[2ip1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IP1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IP1 FirstGlance]. <br> |
- | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Tryptophan--tRNA_ligase Tryptophan--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.2 6.1.1.2] </span>
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</td></tr> |
- | |GENE= WRS1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene></td></tr> |
- | |DOMAIN=<span class='plainlinks'>[http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=cd00806 TrpRS_core]</span>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ip1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ip1 OCA], [https://pdbe.org/2ip1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ip1 RCSB], [https://www.ebi.ac.uk/pdbsum/2ip1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ip1 ProSAT]</span></td></tr> |
- | |RELATEDENTRY=[[1o5t|1O5T]]
| + | </table> |
- | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ip1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ip1 OCA], [http://www.ebi.ac.uk/pdbsum/2ip1 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2ip1 RCSB]</span>
| + | == Function == |
- | }}
| + | [https://www.uniprot.org/uniprot/SYWC_YEAST SYWC_YEAST] |
| + | == Evolutionary Conservation == |
| + | [[Image:Consurf_key_small.gif|200px|right]] |
| + | Check<jmol> |
| + | <jmolCheckbox> |
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ip/2ip1_consurf.spt"</scriptWhenChecked> |
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| + | <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/main_output.php?pdb_ID=2ip1 ConSurf]. |
| + | <div style="clear:both"></div> |
| | | |
- | '''Crystal Structure Analysis of S. cerevisiae Tryptophanyl tRNA Synthetase'''
| + | ==See Also== |
- | | + | *[[Aminoacyl tRNA synthetase 3D structures|Aminoacyl tRNA synthetase 3D structures]] |
- | | + | __TOC__ |
- | ==Overview== | + | </StructureSection> |
- | Saccharomyces cerevisiae is an ideal host from which to obtain high levels of posttranslationally modified eukaryotic proteins for x-ray crystallography. However, extensive replacement of methionine by selenomethionine for anomalous dispersion phasing has proven intractable in yeast. We report a general method to incorporate selenomethionine into proteins expressed in yeast based on manipulation of the appropriate metabolic pathways. sam1(-) sam2(-) mutants, in which the conversion of methionine to S-adenosylmethionine is blocked, exhibit reduced selenomethionine toxicity compared with wild-type yeast, increased production of protein during growth in selenomethionine, and efficient replacement of methionine by selenomethionine, based on quantitative mass spectrometry and x-ray crystallography. The structure of yeast tryptophanyl-tRNA synthetase was solved to 1.8 A by using multiwavelength anomalous dispersion phasing with protein that was expressed and purified from the sam1(-) sam2(-) strain grown in selenomethionine. Six of eight selenium residues were located in the structure.
| + | [[Category: Large Structures]] |
- | | + | |
- | ==About this Structure==
| + | |
- | 2IP1 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IP1 OCA].
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- | | + | |
- | ==Reference==
| + | |
- | Blocking S-adenosylmethionine synthesis in yeast allows selenomethionine incorporation and multiwavelength anomalous dispersion phasing., Malkowski MG, Quartley E, Friedman AE, Babulski J, Kon Y, Wolfley J, Said M, Luft JR, Phizicky EM, DeTitta GT, Grayhack EJ, Proc Natl Acad Sci U S A. 2007 Apr 17;104(16):6678-83. Epub 2007 Apr 10. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17426150 17426150]
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| [[Category: Saccharomyces cerevisiae]] | | [[Category: Saccharomyces cerevisiae]] |
- | [[Category: Single protein]]
| + | [[Category: Malkowski MG]] |
- | [[Category: Tryptophan--tRNA ligase]]
| + | |
- | [[Category: CHTSB, Center for High-Throughput Structural Biology.]]
| + | |
- | [[Category: Malkowski, M G.]] | + | |
- | [[Category: center for high-throughput structural biology]]
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- | [[Category: chtsb]]
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- | [[Category: protein structure initiative]]
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- | [[Category: psi-2]]
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- | [[Category: rossmann fold]]
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- | [[Category: structural genomic]]
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- | | + | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:47:01 2008''
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