1nwd: Difference between revisions

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-[[Image:1nwd.gif|left|200px]]
-<!--
-The line below this paragraph, containing "STRUCTURE_1nwd", creates the "Structure Box" on the page.
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-or leave the SCENE parameter empty for the default display.
--->
-{{STRUCTURE_1nwd|  PDB=1nwd  |  SCENE=  }}
-'''Solution Structure of Ca2+/Calmodulin bound to the C-terminal Domain of Petunia Glutamate Decarboxylase'''
+==Solution Structure of Ca2+/Calmodulin bound to the C-terminal Domain of Petunia Glutamate Decarboxylase==
+<StructureSection load='1nwd' size='340' side='right'caption='[[1nwd]]' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1nwd]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Petunia_x_hybrida Petunia x hybrida] and [https://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NWD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NWD FirstGlance]. <br>
+</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</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=1nwd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nwd OCA], [https://pdbe.org/1nwd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nwd RCSB], [https://www.ebi.ac.uk/pdbsum/1nwd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nwd ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/CALM1_XENLA CALM1_XENLA] 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/nw/1nwd_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=1nwd ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Activation of glutamate decarboxylase (GAD) by calcium-bound calmodulin (CaM) is required for normal plant growth through regulation of gamma-aminobutyrate and glutamate metabolism. The interaction of CaM with the C-terminal domain of GAD is believed to induce dimerization of the enzyme, an event implicated for Ca(2+)-dependent enzyme activation. Here, we present the solution structure of CaM in complex with a dimer of peptides derived from the C-terminus of Petunia hybrida GAD. The 23 kDa ternary complex is pseudo-symmetrical with each domain of CaM bound to one of the two antiparallel GAD peptides, which form an X-shape with an interhelical angle of 60 degrees. To accommodate the dimeric helical GAD target, the two domains of CaM adopt an orientation markedly different from that seen in other CaM-target complexes. Although the dimeric GAD domain is much larger than previously studied CaM-binding peptides, the two CaM domains appear closer together and make a number of interdomain contacts not observed in earlier complexes. The present structure of a single CaM molecule interacting with two target peptides provides new evidence for the conformational flexibility of CaM as well as a structural basis for the ability of CaM to activate two enzyme molecules simultaneously.
-==Overview==
+Structural basis for simultaneous binding of two carboxy-terminal peptides of plant glutamate decarboxylase to calmodulin.,Yap KL, Yuan T, Mal TK, Vogel HJ, Ikura M J Mol Biol. 2003 Apr 18;328(1):193-204. PMID:12684008<ref>PMID:12684008</ref>
-Activation of glutamate decarboxylase (GAD) by calcium-bound calmodulin (CaM) is required for normal plant growth through regulation of gamma-aminobutyrate and glutamate metabolism. The interaction of CaM with the C-terminal domain of GAD is believed to induce dimerization of the enzyme, an event implicated for Ca(2+)-dependent enzyme activation. Here, we present the solution structure of CaM in complex with a dimer of peptides derived from the C-terminus of Petunia hybrida GAD. The 23 kDa ternary complex is pseudo-symmetrical with each domain of CaM bound to one of the two antiparallel GAD peptides, which form an X-shape with an interhelical angle of 60 degrees. To accommodate the dimeric helical GAD target, the two domains of CaM adopt an orientation markedly different from that seen in other CaM-target complexes. Although the dimeric GAD domain is much larger than previously studied CaM-binding peptides, the two CaM domains appear closer together and make a number of interdomain contacts not observed in earlier complexes. The present structure of a single CaM molecule interacting with two target peptides provides new evidence for the conformational flexibility of CaM as well as a structural basis for the ability of CaM to activate two enzyme molecules simultaneously.
-==About this Structure==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-NWD is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Petunia_x_hybrida Petunia x hybrida] and [http://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NWD OCA].
+</div>
+<div class="pdbe-citations 1nwd" style="background-color:#fffaf0;"></div>
-==Reference==
+==See Also==
-Structural basis for simultaneous binding of two carboxy-terminal peptides of plant glutamate decarboxylase to calmodulin., Yap KL, Yuan T, Mal TK, Vogel HJ, Ikura M, J Mol Biol. 2003 Apr 18;328(1):193-204. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12684008 12684008]
+*[[Calmodulin 3D structures|Calmodulin 3D structures]]
-[[Category: Glutamate decarboxylase]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
 [[Category: Petunia x hybrida]]
-[[Category: Protein complex]]
 [[Category: Xenopus laevis]]
-[[Category: Ikura, M.]]
+[[Category: Ikura M]]
-[[Category: Mal, T K.]]
+[[Category: Mal TK]]
-[[Category: Vogel, H J.]]
+[[Category: Vogel HJ]]
-[[Category: Yap, K L.]]
+[[Category: Yap KL]]
-[[Category: Yuan, T.]]
+[[Category: Yuan T]]
-[[Category: Calmodulin]]
-[[Category: Calmodulin-peptide complex]]
-[[Category: Dimer]]
-[[Category: Gad]]
-[[Category: Glutamate decarboxylase]]
-[[Category: Nmr]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 03:03:24 2008''