2z10: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2z10]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Z10 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2Z10 FirstGlance]. <br> | <table><tr><td colspan='2'>[[2z10]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Z10 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2Z10 FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=IYR:3-IODO-TYROSINE'>IYR</scene></td></tr> | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=IYR:3-IODO-TYROSINE'>IYR</scene></td></tr> | ||
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ribosomal-protein-alanine_N-acetyltransferase Ribosomal-protein-alanine N-acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.128 2.3.1.128] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ribosomal-protein-alanine_N-acetyltransferase Ribosomal-protein-alanine N-acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.128 2.3.1.128] </span></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=2z10 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2z10 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2z10 RCSB], [http://www.ebi.ac.uk/pdbsum/2z10 PDBsum], [http://www.topsan.org/Proteins/RSGI/2z10 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=2z10 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2z10 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2z10 RCSB], [http://www.ebi.ac.uk/pdbsum/2z10 PDBsum], [http://www.topsan.org/Proteins/RSGI/2z10 TOPSAN]</span></td></tr> | ||
<table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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[[Category: Ribosomal-protein-alanine N-acetyltransferase]] | [[Category: Ribosomal-protein-alanine N-acetyltransferase]] | ||
[[Category: Thermus thermophilus]] | [[Category: Thermus thermophilus]] | ||
[[Category: Kato-Murayama, M | [[Category: Kato-Murayama, M]] | ||
[[Category: Kuramitsu, S | [[Category: Kuramitsu, S]] | ||
[[Category: Murayama, K | [[Category: Murayama, K]] | ||
[[Category: | [[Category: Structural genomic]] | ||
[[Category: Shirouzu, M | [[Category: Shirouzu, M]] | ||
[[Category: Terada, T | [[Category: Terada, T]] | ||
[[Category: Yokoyama, S | [[Category: Yokoyama, S]] | ||
[[Category: Acyltransferase]] | [[Category: Acyltransferase]] | ||
[[Category: Alpha/beta protein]] | [[Category: Alpha/beta protein]] | ||
[[Category: National project on protein structural and functional analyse]] | [[Category: National project on protein structural and functional analyse]] | ||
[[Category: Nppsfa]] | [[Category: Nppsfa]] | ||
[[Category: Rsgi]] | [[Category: Rsgi]] | ||
[[Category: Transferase]] | [[Category: Transferase]] |
Revision as of 14:30, 20 January 2015
Crystal structure of putative acetyltransferaseCrystal structure of putative acetyltransferase
Structural highlights
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 PubMedWe developed an Escherichia coli cell-based system to generate proteins containing 3-iodo-l-tyrosine at desired sites, and we used this system for structure determination by single-wavelength anomalous dispersion (SAD) phasing with the strong iodine signal. Tyrosyl-tRNA synthetase from Methanocaldococcus jannaschii was engineered to specifically recognize 3-iodo-l-tyrosine. The 1.7 A crystal structure of the engineered variant, iodoTyrRS-mj, bound with 3-iodo-l-tyrosine revealed the structural basis underlying the strict specificity for this nonnatural substrate; the iodine moiety makes van der Waals contacts with 5 residues at the binding pocket. E. coli cells expressing iodoTyrRS-mj and the suppressor tRNA were used to incorporate 3-iodo-l-tyrosine site specifically into the ribosomal protein N-acetyltransferase from Thermus thermophilus. The crystal structure of this enzyme with iodotyrosine was determined at 1.8 and 2.2 A resolutions by SAD phasing at CuKalpha and CrKalpha wavelengths, respectively. The native structure, determined by molecular replacement, revealed no significant structural distortion caused by iodotyrosine incorporation. Genetic Encoding of 3-Iodo-l-Tyrosine in Escherichia coli for Single-Wavelength Anomalous Dispersion Phasing in Protein Crystallography.,Sakamoto K, Murayama K, Oki K, Iraha F, Kato-Murayama M, Takahashi M, Ohtake K, Kobayashi T, Kuramitsu S, Shirouzu M, Yokoyama S Structure. 2009 Mar 11;17(3):335-44. PMID:19278648[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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