2rhs: Difference between revisions

← Older edit

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 3: / Line 3: @@
 <StructureSection load='2rhs' size='340' side='right'caption='[[2rhs]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2rhs]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_29970 Atcc 29970]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RHS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RHS FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2rhs]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_haemolyticus Staphylococcus haemolyticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RHS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RHS FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GAX:1-{3-[(4-PYRIDIN-2-YLPIPERAZIN-1-YL)SULFONYL]PHENYL}-3-(1,3-THIAZOL-2-YL)UREA'>GAX</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 2.2&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2rhq|2rhq]]</div></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GAX:1-{3-[(4-PYRIDIN-2-YLPIPERAZIN-1-YL)SULFONYL]PHENYL}-3-(1,3-THIAZOL-2-YL)UREA'>GAX</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pheS ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1283 ATCC 29970]), pheT ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1283 ATCC 29970])</td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Phenylalanine--tRNA_ligase Phenylalanine--tRNA ligase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.20 6.1.1.20] </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=2rhs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rhs OCA], [https://pdbe.org/2rhs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rhs RCSB], [https://www.ebi.ac.uk/pdbsum/2rhs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rhs ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/SYFA_STAHJ SYFA_STAHJ]
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 20: / Line 20: @@
 </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=2rhs ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-In this article, we describe for the first time the high-resolution crystal structure of a phenylalanine tRNA synthetase from the pathogenic bacterium Staphylococcus haemolyticus. We demonstrate the subtle yet important structural differences between this enzyme and the previously described Thermus thermophilus ortholog. We also explain the structure-activity relationship of several recently reported inhibitors. The native enzyme crystals were of poor quality--they only diffracted X-rays to 3-5A resolution. Therefore, we have executed a rational surface mutagenesis strategy that has yielded crystals of this 2300-amino acid multidomain protein, diffracting to 2A or better. This methodology is discussed and contrasted with the more traditional domain truncation approach.
-Rational protein engineering in action: the first crystal structure of a phenylalanine tRNA synthetase from Staphylococcus haemolyticus.,Evdokimov AG, Mekel M, Hutchings K, Narasimhan L, Holler T, McGrath T, Beattie B, Fauman E, Yan C, Heaslet H, Walter R, Finzel B, Ohren J, McConnell P, Braden T, Sun F, Spessard C, Banotai C, Al-Kassim L, Ma W, Wengender P, Kole D, Garceau N, Toogood P, Liu J J Struct Biol. 2008 Apr;162(1):152-69. Epub 2007 Nov 13. PMID:18086534<ref>PMID:18086534</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 2rhs" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Aminoacyl tRNA synthetase 3D structures|Aminoacyl tRNA synthetase 3D structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Atcc 29970]]
 [[Category: Large Structures]]
-[[Category: Phenylalanine--tRNA ligase]]
+[[Category: Staphylococcus haemolyticus]]
-[[Category: Evdokimov, A G]]
+[[Category: Evdokimov AG]]
-[[Category: Mekel, M]]
+[[Category: Mekel M]]
-[[Category: Aminoacyl-trna synthetase]]
-[[Category: Atp-binding]]
-[[Category: Cytoplasm]]
-[[Category: Heterotetramer]]
-[[Category: Ligase]]
-[[Category: Magnesium]]
-[[Category: Metal-binding]]
-[[Category: Nucleotide-binding]]
-[[Category: Phenylalanine]]
-[[Category: Protein biosynthesis]]
-[[Category: Rna-binding]]
-[[Category: Trna]]
-[[Category: Trna-binding]]