1wls: Difference between revisions

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-[[Image:1wls.png|left|200px]]
-{{STRUCTURE_1wls|  PDB=1wls  |  SCENE=  }}
+==Crystal structure of L-asparaginase I homologue protein from Pyrococcus horikoshii==
+<StructureSection load='1wls' size='340' side='right'caption='[[1wls]], [[Resolution|resolution]] 2.16&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1wls]] is a 2 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=1WLS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WLS FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.16&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=1wls FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wls OCA], [https://pdbe.org/1wls PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wls RCSB], [https://www.ebi.ac.uk/pdbsum/1wls PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wls ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/O57797_PYRHO O57797_PYRHO]
+== 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/wl/1wls_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1wls ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The crystal structure of the L-asparaginase from the hyperthermophilic archaeon Pyrococcus horikoshii (PhA) was determined by the multiwavelength anomalous diffraction (MAD) method and was refined to a resolution of 2.16 angstroms with a crystallographic R factor and free R factor of 21.1 and 25.3%, respectively. This is the first report of the three-dimensional structure of a type I L-asparaginase. These enyzmes are known as cytosolic L-asparaginases with lower affinities for substrate than the type II L-asparaginases. Although the overall fold of PhA was closely related to the structure of the well characterized type II L-asparaginase, structural differences were also detected. PhA forms a homodimer that corresponds to half the homotetramer of type II L-asparaginases. Structure comparison at the active site reveals that most catalytic residues are conserved except for two residues that recognize the amino group of the substrate. Additionally, a remarkable structural difference is found in the so-called 'active-site flexible loop'. In PhA this loop is stabilized by beta-hairpin formation and by elaborate interactions with the type-I-specific alpha-helical region derived from the other subunit forming the PhA dimer. The flexible loop of the type II enzyme is considered to serve as a mobile gate to the active site. Therefore, the loop stabilization observed in the PhA structure may cause limitation of the access of the substrate to the active site.
-===Crystal structure of L-asparaginase I homologue protein from Pyrococcus horikoshii===
+Structure of the type I L-asparaginase from the hyperthermophilic archaeon Pyrococcus horikoshii at 2.16 angstroms resolution.,Yao M, Yasutake Y, Morita H, Tanaka I Acta Crystallogr D Biol Crystallogr. 2005 Mar;61(Pt 3):294-301. Epub 2005, Feb 24. PMID:15735339<ref>PMID:15735339</ref>
-{{ABSTRACT_PUBMED_15735339}}
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 1wls" style="background-color:#fffaf0;"></div>
-==About this Structure==
+==See Also==
-[[1wls]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Pyrococcus_horikoshii Pyrococcus horikoshii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WLS OCA].
+*[[Asparaginase 3D structures|Asparaginase 3D structures]]
+== References ==
-==Reference==
+<references/>
-<ref group="xtra">PMID:015735339</ref><references group="xtra"/>
+__TOC__
-[[Category: Asparaginase]]
+</StructureSection>
+[[Category: Large Structures]]
 [[Category: Pyrococcus horikoshii]]
-[[Category: Morita, H.]]
+[[Category: Morita H]]
-[[Category: Tanaka, I.]]
+[[Category: Tanaka I]]
-[[Category: Yao, M.]]
+[[Category: Yao M]]
-[[Category: Yasutake, Y.]]
+[[Category: Yasutake Y]]
-[[Category: Hydrolase]]
-[[Category: Structural genomic]]