2pq3: Difference between revisions

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New page: left|200px<br /><applet load="2pq3" size="350" color="white" frame="true" align="right" spinBox="true" caption="2pq3, resolution 1.30Å" /> '''N-Terminal Calmoduli...
 
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'''N-Terminal Calmodulin Zn-Trapped Intermediate'''<br />


==Overview==
==N-Terminal Calmodulin Zn-Trapped Intermediate==
Calmodulin (CaM) is a 16.8-kDa calcium-binding protein involved in, calcium-signal transduction. It is the canonical member of the EF-hand, family of proteins, which are characterized by a helix-loop-helix, calcium-binding motif. CaM is composed of N- and C-terminal globular, domains (N-CaM and C-CaM), and within each domain there are two EF-hand, motifs. Upon binding calcium, CaM undergoes a significant, global, conformational change involving reorientation of the four helix bundles in, each of its two domains. This conformational change upon ion binding is a, key component of the signal transduction and regulatory roles of CaM, yet, the precise nature of this transition is still unclear. Here, we present a, 1.3-A structure of zinc-bound N-terminal calmodulin (N-CaM) solved by, single-wavelength anomalous diffraction phasing of a selenomethionyl, N-CaM. Our zinc-bound N-CaM structure differs from previously reported CaM, structures and resembles calcium-free apo-calmodulin (apo-CaM), despite, the zinc binding to both EF-hand motifs. Structural comparison with, calcium-free apo-CaM, calcium-loaded CaM, and a cross-linked, calcium-loaded CaM suggests that our zinc-bound N-CaM reveals an, intermediate step in the initiation of metal ion binding at the first, EF-hand motif. Our data also suggest that metal ion coordination by two, key residues in the first metal-binding site represents an initial step in, the conformational transition induced by metal binding. This is followed, by reordering of the N-terminal region of the helix exiting from this, first binding loop. This conformational switch should be incorporated into, models of either stepwise conformational transition or flexible, dynamic, energetic state sampling-based transition.
<StructureSection load='2pq3' size='340' side='right'caption='[[2pq3]], [[Resolution|resolution]] 1.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2pq3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PQ3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PQ3 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]] 1.3&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CAC:CACODYLATE+ION'>CAC</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=2pq3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pq3 OCA], [https://pdbe.org/2pq3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2pq3 RCSB], [https://www.ebi.ac.uk/pdbsum/2pq3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2pq3 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CALM1_RAT CALM1_RAT] Calmodulin mediates the control of a large number of enzymes, ion channels, aquaporins and other proteins through calcium-binding. Among the enzymes to be stimulated by the calmodulin-calcium complex are a number of protein kinases and phosphatases. Together with CCP110 and centrin, is involved in a genetic pathway that regulates the centrosome cycle and progression through cytokinesis. Mediates calcium-dependent inactivation of CACNA1C. Positively regulates calcium-activated potassium channel activity of KCNN2.[UniProtKB:P62158]
== 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/pq/2pq3_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=2pq3 ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
2PQ3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=CAC:'>CAC</scene> and <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PQ3 OCA].
*[[Calmodulin 3D structures|Calmodulin 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
A 1.3-A structure of zinc-bound N-terminal domain of calmodulin elucidates potential early ion-binding step., Warren JT, Guo Q, Tang WJ, J Mol Biol. 2007 Nov 23;374(2):517-27. Epub 2007 Sep 21. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17942116 17942116]
[[Category: Large Structures]]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
[[Category: Single protein]]
[[Category: Guo Q]]
[[Category: Guo, Q.]]
[[Category: Tang WJ]]
[[Category: Tang, W.J.]]
[[Category: Warren JT]]
[[Category: Warren, J.T.]]
[[Category: CAC]]
[[Category: ZN]]
[[Category: calmodulin]]
[[Category: cam]]
[[Category: ef-hand]]
[[Category: helix-turn-helix]]
[[Category: metal binding protein]]
[[Category: n-cam]]
[[Category: n-terminal calmodulin]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 10:42:59 2008''

Latest revision as of 12:11, 21 February 2024

N-Terminal Calmodulin Zn-Trapped IntermediateN-Terminal Calmodulin Zn-Trapped Intermediate

Structural highlights

2pq3 is a 1 chain structure with sequence from Rattus norvegicus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.3Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CALM1_RAT Calmodulin mediates the control of a large number of enzymes, ion channels, aquaporins and other proteins through calcium-binding. Among the enzymes to be stimulated by the calmodulin-calcium complex are a number of protein kinases and phosphatases. Together with CCP110 and centrin, is involved in a genetic pathway that regulates the centrosome cycle and progression through cytokinesis. Mediates calcium-dependent inactivation of CACNA1C. Positively regulates calcium-activated potassium channel activity of KCNN2.[UniProtKB:P62158]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

2pq3, resolution 1.30Å

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