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2pq3

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Revision as of 08:31, 29 August 2018

N-Terminal Calmodulin Zn-Trapped Intermediate

Structural highlights

2pq3 is a 1 chain structure with sequence from Buffalo rat. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Gene:	Calm1, Calm, Cam, Cam1 (Buffalo rat)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Evolutionary Conservation

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

Publication Abstract from PubMed

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.

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:17942116^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Warren JT, Guo Q, Tang WJ. A 1.3-A structure of zinc-bound N-terminal domain of calmodulin elucidates potential early ion-binding step. J Mol Biol. 2007 Nov 23;374(2):517-27. Epub 2007 Sep 21. PMID:17942116 doi:10.1016/j.jmb.2007.09.048

1 Structural highlights
2 Evolutionary Conservation
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2pq3"

@@ Line 1: / Line 1: @@
 ==N-Terminal Calmodulin Zn-Trapped Intermediate==
 <StructureSection load='2pq3' size='340' side='right' caption='[[2pq3]], [[Resolution|resolution]] 1.30&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CAC:CACODYLATE+ION'>CAC</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Calm1, Calm, Cam, Cam1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2pq3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pq3 OCA], [http://pdbe.org/2pq3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2pq3 RCSB], [http://www.ebi.ac.uk/pdbsum/2pq3 PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2pq3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pq3 OCA], [http://pdbe.org/2pq3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2pq3 RCSB], [http://www.ebi.ac.uk/pdbsum/2pq3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2pq3 ProSAT]</span></td></tr>
 </table>
 == Evolutionary Conservation ==
@@ Line 11: / Line 12: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pq/2pq3_consurf.spt"</scriptWhenChecked>
+    <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>

2pq3

From Proteopedia

Revision as of 08:31, 29 August 2018

N-Terminal Calmodulin Zn-Trapped Intermediate

Structural highlights

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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