2k7k: Difference between revisions

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-{{Seed}}
-[[Image:2k7k.png|left|200px]]
-<!--
+==Human Acylphosphatase (AcPh) common type==
-The line below this paragraph, containing "STRUCTURE_2k7k", creates the "Structure Box" on the page.
+<StructureSection load='2k7k' size='340' side='right'caption='[[2k7k]]' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[2k7k]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2K7K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2K7K FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2k7k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k7k OCA], [https://pdbe.org/2k7k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2k7k RCSB], [https://www.ebi.ac.uk/pdbsum/2k7k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2k7k ProSAT]</span></td></tr>
-{{STRUCTURE_2k7k|  PDB=2k7k  |  SCENE=  }}
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/ACYP1_HUMAN ACYP1_HUMAN] Its physiological role is not yet clear.
+== 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/k7/2k7k_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=2k7k ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Here, we report the application of a computational approach that allows the rational design of enzymes with enhanced thermostability while retaining full enzymatic activity. The approach is based on the optimization of the energy of charge-charge interactions on the protein surface. We experimentally tested the validity of the approach on 2 human enzymes, acylphosphatase (AcPh) and Cdc42 GTPase, that differ in size (98 vs. 198-aa residues, respectively) and tertiary structure. We show that the designed proteins are significantly more stable than the corresponding WT proteins. The increase in stability is not accompanied by significant changes in structure, oligomerization state, or, most importantly, activity of the designed AcPh or Cdc42. This success of the design methodology suggests that it can be universally applied to other enzymes, on its own or in combination with the other strategies based on redesign of the interactions in the protein core.
-===Human Acylphosphatase (AcPh) common type===
+Rational stabilization of enzymes by computational redesign of surface charge-charge interactions.,Gribenko AV, Patel MM, Liu J, McCallum SA, Wang C, Makhatadze GI Proc Natl Acad Sci U S A. 2009 Feb 5. PMID:19196981<ref>PMID:19196981</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-<!--
+</div>
-The line below this paragraph, {{ABSTRACT_PUBMED_19196981}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 2k7k" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 19196981 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_19196981}}
+__TOC__
+</StructureSection>
-==About this Structure==
-K7K is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2K7K OCA].
-==Reference==
-Rational stabilization of enzymes by computational redesign of surface charge-charge interactions., Gribenko AV, Patel MM, Liu J, McCallum SA, Wang C, Makhatadze GI, Proc Natl Acad Sci U S A. 2009 Feb 5. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/19196981 19196981]
-[[Category: Acylphosphatase]]
 [[Category: Homo sapiens]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Pdbx_ordinal=, <PDBx:audit_author.]]
+[[Category: Gribenko AV]]
-[[Category: Acetylation]]
+[[Category: Liu J]]
-[[Category: Hydrolase]]
+[[Category: Makhatadze GI]]
-[[Category: Protein]]
+[[Category: McCallum SA]]
+[[Category: Patel MM]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Mar 11 20:16:51 2009''
+[[Category: Wang C]]