1m15: Difference between revisions

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-[[Image:1m15.gif|left|200px]]
- {{Structure
+==Transition state structure of arginine kinase==
-|PDB= 1m15 |SIZE=350|CAPTION= <scene name='initialview01'>1m15</scene>, resolution 1.20&Aring;
+<StructureSection load='1m15' size='340' side='right'caption='[[1m15]], [[Resolution|resolution]] 1.20&Aring;' scene=''>
-|SITE=
+== Structural highlights ==
-|LIGAND= <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ARG:ARGININE'>ARG</scene> and <scene name='pdbligand=ADP:ADENOSINE-5'-DIPHOSPHATE'>ADP</scene>
+<table><tr><td colspan='2'>[[1m15]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Limulus_polyphemus Limulus polyphemus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M15 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1M15 FirstGlance]. <br>
-|ACTIVITY= [http://en.wikipedia.org/wiki/Transferase Transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.3.3. 2.7.3.3.]
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.2&#8491;</td></tr>
-|GENE=
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=ARG:ARGININE'>ARG</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</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=1m15 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m15 OCA], [https://pdbe.org/1m15 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1m15 RCSB], [https://www.ebi.ac.uk/pdbsum/1m15 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1m15 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/KARG_LIMPO KARG_LIMPO]
+== 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/m1/1m15_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=1m15 ConSurf].
+<div style="clear:both"></div>
-'''TRANSITION STATE STRUCTURE OF ARGININE KINASE'''
+==See Also==
+*[[Arginine kinase 3D structures|Arginine kinase 3D structures]]
+__TOC__
-==Overview==
+</StructureSection>
-The three-dimensional crystal structure of an arginine kinase transition-state analogue complex has been refined at 1.2 A resolution, with an overall R factor of 12.3%. The current model provides a unique opportunity to analyze the structure of a bimolecular (phosphagen kinase) enzyme in its transition state. This atomic resolution structure confirms in-line transfer of the phosphoryl group and the catalytic importance of the precise alignment of the substrates. The structure is consistent with a concerted proton transfer that has been proposed for an unrelated kinase. Refinement of anisotropic temperature factors and translation-libration-screw (TLS) analyses led to the identification of four rigid groups and their prevalent modes of motion in the transition state. The relative magnitudes of the mobility of rigid groups are consistent with their proposed roles in catalysis.
+[[Category: Large Structures]]
-==About this Structure==
-M15 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Limulus_polyphemus Limulus polyphemus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M15 OCA].
-==Reference==
-Refinement of the arginine kinase transition-state analogue complex at 1.2 A resolution: mechanistic insights., Yousef MS, Fabiola F, Gattis JL, Somasundaram T, Chapman MS, Acta Crystallogr D Biol Crystallogr. 2002 Dec;58(Pt 12):2009-17. Epub 2002, Nov 23. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12454458 12454458]
 [[Category: Limulus polyphemus]]
-[[Category: Single protein]]
+[[Category: Chapman MS]]
-[[Category: Transferase]]
+[[Category: Fabiola F]]
-[[Category: Chapman, M S.]]
+[[Category: Gattis JL]]
-[[Category: Fabiola, F.]]
+[[Category: Somasundaram T]]
-[[Category: Gattis, J L.]]
+[[Category: Yousef MS]]
-[[Category: Somasundaram, T.]]
-[[Category: Yousef, M S.]]
-[[Category: ADP]]
-[[Category: ARG]]
-[[Category: MG]]
-[[Category: NO3]]
-[[Category: adenosine triphosphate]]
-[[Category: arginine kinase]]
-[[Category: creatine kinase]]
-[[Category: phosphagen kinase]]
-[[Category: transition state analog]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:37:35 2008''