1hfk: Difference between revisions

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-[[Image:1hfk.gif|left|200px]]<br />
-<applet load="1hfk" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1hfk, resolution 2.17&Aring;" />
-'''ASPARAGINASE FROM ERWINIA CHRYSANTHEMI, HEXAGONAL FORM WITH WEAK SULFATE'''<br />
-==Overview==
+==Asparaginase from Erwinia chrysanthemi, hexagonal form with weak sulfate==
-Quasi-enantiomorphic crystals of the Y25F mutant of Escherichia coli, L-asparaginase and of the native Erwinia chrysanthemi L-asparaginase were, obtained in the hexagonal space groups P6(5)22 and P6(1)22, respectively., The structures of these highly homologous enzymes were solved by molecular, replacement and were refined with data extending to 2.2-2.5 A. These, structures were compared with each other, as well as with other, L-asparaginase structures previously observed with different crystal, packing. It is concluded that the observed phenomenon, which is rare, was, most likely to have arisen by chance.
+<StructureSection load='1hfk' size='340' side='right'caption='[[1hfk]], [[Resolution|resolution]] 2.17&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1hfk]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Dickeya_chrysanthemi Dickeya chrysanthemi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HFK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HFK 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]] 2.17&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=1hfk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hfk OCA], [https://pdbe.org/1hfk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hfk RCSB], [https://www.ebi.ac.uk/pdbsum/1hfk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hfk ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/ASPG_DICCH ASPG_DICCH]
+== 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/hf/1hfk_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=1hfk ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Quasi-enantiomorphic crystals of the Y25F mutant of Escherichia coli L-asparaginase and of the native Erwinia chrysanthemi L-asparaginase were obtained in the hexagonal space groups P6(5)22 and P6(1)22, respectively. The structures of these highly homologous enzymes were solved by molecular replacement and were refined with data extending to 2.2-2.5 A. These structures were compared with each other, as well as with other L-asparaginase structures previously observed with different crystal packing. It is concluded that the observed phenomenon, which is rare, was most likely to have arisen by chance.
-==About this Structure==
+Structures of two highly homologous bacterial L-asparaginases: a case of enantiomorphic space groups.,Jaskolski M, Kozak M, Lubkowski J, Palm G, Wlodawer A Acta Crystallogr D Biol Crystallogr. 2001 Mar;57(Pt 3):369-77. PMID:11223513<ref>PMID:11223513</ref>
-HFK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Erwinia_chrysanthemi Erwinia chrysanthemi] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Asparaginase Asparaginase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.1 3.5.1.1] Structure known Active Sites: AS1 and AS2. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HFK OCA].
-==Reference==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-Structures of two highly homologous bacterial L-asparaginases: a case of enantiomorphic space groups., Jaskolski M, Kozak M, Lubkowski J, Palm G, Wlodawer A, Acta Crystallogr D Biol Crystallogr. 2001 Mar;57(Pt 3):369-77. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11223513 11223513]
+</div>
-[[Category: Asparaginase]]
+<div class="pdbe-citations 1hfk" style="background-color:#fffaf0;"></div>
-[[Category: Erwinia chrysanthemi]]
-[[Category: Single protein]]
-[[Category: Jaskolski, M.]]
-[[Category: Kozak, M.]]
-[[Category: Lubkowski, J.]]
-[[Category: Palm, G.J.]]
-[[Category: Wlodawer, A.]]
-[[Category: SO4]]
-[[Category: hydrolase]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov  5 15:00:05 2007''
+==See Also==
+*[[Asparaginase 3D structures|Asparaginase 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Dickeya chrysanthemi]]
+[[Category: Large Structures]]
+[[Category: Jaskolski M]]
+[[Category: Kozak M]]
+[[Category: Lubkowski J]]
+[[Category: Palm GJ]]
+[[Category: Wlodawer A]]