1mxe: Difference between revisions

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-[[Image:1mxe.gif|left|200px]]
-<!--
+==Structure of the Complex of Calmodulin with the Target Sequence of CaMKI==
-The line below this paragraph, containing "STRUCTURE_1mxe", creates the "Structure Box" on the page.
+<StructureSection load='1mxe' size='340' side='right'caption='[[1mxe]], [[Resolution|resolution]] 1.70&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'>[[1mxe]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster] and [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MXE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MXE 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]] 1.7&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
-{{STRUCTURE_1mxe|  PDB=1mxe  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1mxe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mxe OCA], [https://pdbe.org/1mxe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mxe RCSB], [https://www.ebi.ac.uk/pdbsum/1mxe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mxe ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/CALM_DROME CALM_DROME] Calmodulin mediates the control of a large number of enzymes, ion channels and other proteins by Ca(2+). Among the enzymes to be stimulated by the calmodulin-Ca(2+) complex are a number of protein kinases and phosphatases.
+== 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/mx/1mxe_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=1mxe ConSurf].
+<div style="clear:both"></div>
-'''Structure of the Complex of Calmodulin with the Target Sequence of CaMKI'''
+==See Also==
+*[[Calmodulin 3D structures|Calmodulin 3D structures]]
+__TOC__
-==Overview==
+</StructureSection>
-Calcium-saturated calmodulin (CaM) directly activates CaM-dependent protein kinase I (CaMKI) by binding to a region in the C-terminal regulatory sequence of the enzyme to relieve autoinhibition. The structure of CaM in a high-affinity complex with a 25-residue peptide of CaMKI (residues 294-318) has been determined by X-ray crystallography at 1.7 A resolution. Upon complex formation, the CaMKI peptide adopts an alpha-helical conformation, while changes in the CaM domain linker enable both its N- and C-domains to wrap around the peptide helix. Target peptide residues Trp-303 (interacting with the CaM C-domain) and Met-316 (with the CaM N-domain) define the mode of binding as 1-14. In addition, two basic patches on the peptide form complementary charge interactions with CaM. The CaM-peptide affinity is approximately 1 pM, compared with 30 nM for the CaM-kinase complex, indicating that activation of autoinhibited CaMKI by CaM requires a costly energetic disruption of the interactions between the CaM-binding sequence and the rest of the enzyme. We present biochemical and structural evidence indicating the involvement of both CaM domains in the activation process: while the C-domain exhibits tight binding toward the regulatory sequence, the N-domain is necessary for activation. Our crystal structure also enables us to identify the full CaM-binding sequence. Residues Lys-296 and Phe-298 from the target peptide interact directly with CaM, demonstrating overlap between the autoinhibitory and CaM-binding sequences. Thus, the kinase activation mechanism involves the binding of CaM to residues associated with the inhibitory pseudosubstrate sequence.
-==About this Structure==
-MXE is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MXE OCA].
-==Reference==
-Structure of the complex of calmodulin with the target sequence of calmodulin-dependent protein kinase I: studies of the kinase activation mechanism., Clapperton JA, Martin SR, Smerdon SJ, Gamblin SJ, Bayley PM, Biochemistry. 2002 Dec 17;41(50):14669-79. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12475216 12475216]
-[[Category: Calcium/calmodulin-dependent protein kinase]]
 [[Category: Drosophila melanogaster]]
-[[Category: Protein complex]]
+[[Category: Large Structures]]
-[[Category: Bayley, P M.]]
+[[Category: Rattus norvegicus]]
-[[Category: Clapperton, J A.]]
+[[Category: Bayley PM]]
-[[Category: Gamblin, S J.]]
+[[Category: Clapperton JA]]
-[[Category: Martin, S R.]]
+[[Category: Gamblin SJ]]
-[[Category: Smerdon, S J.]]
+[[Category: Martin SR]]
-[[Category: Calmodulin]]
+[[Category: Smerdon SJ]]
-[[Category: Calmodulin-pepide complex]]
-[[Category: Camki]]
-[[Category: Xray]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 01:50:11 2008''