1e4y: Difference between revisions

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-[[Image:1e4y.png|left|200px]]
-<!--
+==Mutant P9L of adenylate kinase from E. coli, modified in the Gly-loop==
-The line below this paragraph, containing "STRUCTURE_1e4y", creates the "Structure Box" on the page.
+<StructureSection load='1e4y' size='340' side='right'caption='[[1e4y]], [[Resolution|resolution]] 1.85&Aring;' 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'>[[1e4y]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E4Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1E4Y 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">X-ray diffraction, [[Resolution|Resolution]] 1.85&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AP5:BIS(ADENOSINE)-5-PENTAPHOSPHATE'>AP5</scene></td></tr>
-{{STRUCTURE_1e4y|  PDB=1e4y  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1e4y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e4y OCA], [https://pdbe.org/1e4y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1e4y RCSB], [https://www.ebi.ac.uk/pdbsum/1e4y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1e4y ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/KAD_ECOLI KAD_ECOLI] Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. This small ubiquitous enzyme involved in the energy metabolism and nucleotide synthesis, is essential for maintenance and cell growth.[HAMAP-Rule:MF_00235]
+== 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/e4/1e4y_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=1e4y ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Two mutants of adenylate kinase from Escherichia coli have been crystallized and analyzed by X-ray diffraction at resolutions of 3.4 and 2.4 A, respectively. These mutants are Pro-9--&gt;Leu and Gly-10--&gt;Val. They were selected for their positions in the highly conserved Gly-loop forming a giant anion hole for the beta-phosphate of ATP (GTP) in adenylate kinases, H-ras-p21, and other nucleotide-binding proteins. Mutants at these positions of H-ras-p21 cause cancer. In adenylate kinase these mutations cause smallish changes at the active site. Relating the structural changes to the known changes in catalysis indicates that these mutants hinder the induced-fit movements. As a side result we find that mutant Pro-9--&gt;Leu and wild-type form one very similar crystal packing contact that is crystallographic in one case and noncrystallographic in the other, while all other packing contacts and the space groups are quite at variance.
-===MUTANT P9L OF ADENYLATE KINASE FROM E. COLI, MODIFIED IN THE GLY-LOOP===
+Crystal structures of two mutants of adenylate kinase from Escherichia coli that modify the Gly-loop.,Muller CW, Schulz GE Proteins. 1993 Jan;15(1):42-9. PMID:8451239<ref>PMID:8451239</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_8451239}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 1e4y" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 8451239 is the PubMed ID number.
--->
-{{ABSTRACT_PUBMED_8451239}}
-==About this Structure==
-[[1e4y]] is a 2 chain structure of [[Adenylate kinase]] with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E4Y OCA].
 ==See Also==
-*[[Adenylate kinase]]
+*[[Adenylate kinase 3D structures|Adenylate kinase 3D structures]]
+== References ==
-==Reference==
+<references/>
-<ref group="xtra">PMID:8451239</ref><ref group="xtra">PMID:2162964</ref><ref group="xtra">PMID:2845103</ref><references group="xtra"/>
+__TOC__
-[[Category: Adenylate kinase]]
+</StructureSection>
 [[Category: Escherichia coli]]
-[[Category: Mueller, C W.]]
+[[Category: Large Structures]]
-[[Category: Schulz, G E.]]
+[[Category: Mueller CW]]
+[[Category: Schulz GE]]