1e4v: Difference between revisions

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-[[Image:1e4v.jpg|left|200px]]
-<!--
-The line below this paragraph, containing "STRUCTURE_1e4v", creates the "Structure Box" on the page.
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-{{STRUCTURE_1e4v|  PDB=1e4v  |  SCENE=  }}
-'''MUTANT G10V OF ADENYLATE KINASE FROM E. COLI, MODIFIED IN THE GLY-LOOP'''
+==Mutant G10V of adenylate kinase from E. coli, modified in the Gly-loop==
+<StructureSection load='1e4v' size='340' side='right'caption='[[1e4v]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1e4v]] 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=1E4V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1E4V 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]] 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>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1e4v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e4v OCA], [https://pdbe.org/1e4v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1e4v RCSB], [https://www.ebi.ac.uk/pdbsum/1e4v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1e4v 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/e4/1e4v_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=1e4v 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.
-==Overview==
+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>
-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.
-==About this Structure==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-E4V is a [[Single protein]] structure of 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=1E4V OCA].
+</div>
+<div class="pdbe-citations 1e4v" style="background-color:#fffaf0;"></div>
-==Reference==
+==See Also==
-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:[http://www.ncbi.nlm.nih.gov/pubmed/8451239 8451239]
+*[[Adenylate kinase 3D structures|Adenylate kinase 3D structures]]
-[[Category: Adenylate kinase]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Escherichia coli]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Mueller, C W.]]
+[[Category: Mueller CW]]
-[[Category: Schulz, G E.]]
+[[Category: Schulz GE]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 14:39:53 2008''