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2pq3

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[[Image:2pq3.gif|left|200px]]<br /><applet load="2pq3" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2pq3.gif|left|200px]]
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caption="2pq3, resolution 1.30&Aring;" />
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'''N-Terminal Calmodulin Zn-Trapped Intermediate'''<br />
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{{Structure
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|PDB= 2pq3 |SIZE=350|CAPTION= <scene name='initialview01'>2pq3</scene>, resolution 1.30&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=CAC:CACODYLATE+ION'>CAC</scene> and <scene name='pdbligand=ZN:ZINC ION'>ZN</scene>
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|ACTIVITY=
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|GENE= Calm1, Calm, Cam, Cam1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus])
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}}
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'''N-Terminal Calmodulin Zn-Trapped Intermediate'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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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].
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2PQ3 is a [[Single protein]] structure of sequence from [http://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].
==Reference==
==Reference==
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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]
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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://www.ncbi.nlm.nih.gov/pubmed/17942116 17942116]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: n-terminal calmodulin]]
[[Category: n-terminal calmodulin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:31:56 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:16:04 2008''

Revision as of 16:16, 20 March 2008

Image:2pq3.gif


PDB ID 2pq3

Drag the structure with the mouse to rotate
, resolution 1.30Å
Ligands: and
Gene: Calm1, Calm, Cam, Cam1 (Rattus norvegicus)
Coordinates: save as pdb, mmCIF, xml



N-Terminal Calmodulin Zn-Trapped Intermediate


Overview

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.

About this Structure

2PQ3 is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.

Reference

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

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