2ix7

From Proteopedia

(Difference between revisions)

Current revision

Structure of apo-calmodulin bound to unconventional myosin V

Structural highlights

2ix7 is a 3 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.5Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CALM1_MOUSE Calmodulin acts as part of a calcium signal transduction pathway by mediating the control of a large number of enzymes, ion channels, aquaporins and other proteins through calcium-binding. Calcium-binding is required for the activation of calmodulin. Among the enzymes to be stimulated by the calmodulin-calcium complex are a number of protein kinases, such as myosin light-chain kinases and calmodulin-dependent protein kinase type II (CaMK2), and phosphatases. Together with CCP110 and centrin, is involved in a genetic pathway that regulates the centrosome cycle and progression through cytokinesis. Is a regulator of voltage-dependent L-type calcium channels. Mediates calcium-dependent inactivation of CACNA1C. Positively regulates calcium-activated potassium channel activity of KCNN2. Forms a potassium channel complex with KCNQ1 and regulates electrophysiological activity of the channel via calcium-binding. Acts as a sensor to modulate the endoplasmic reticulum contacts with other organelles mediated by VMP1:ATP2A2.[UniProtKB:P0DP23]

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

A 2.5-A resolution structure of calcium-free calmodulin (CaM) bound to the first two IQ motifs of the murine myosin V heavy chain reveals an unusual CaM conformation. The C-terminal lobe of each CaM adopts a semi-open conformation that grips the first part of the IQ motif (IQxxxR), whereas the N-terminal lobe adopts a closed conformation that interacts more weakly with the second part of the motif (GxxxR). Variable residues in the IQ motif play a critical role in determining the precise structure of the bound CaM, such that even the consensus residues of different motifs show unique interactions with CaM. This complex serves as a model for the lever arm region of many classes of unconventional myosins, as well as other IQ motif-containing proteins such as neuromodulin and IQGAPs.

Crystal structure of apo-calmodulin bound to the first two IQ motifs of myosin V reveals essential recognition features.,Houdusse A, Gaucher JF, Krementsova E, Mui S, Trybus KM, Cohen C Proc Natl Acad Sci U S A. 2006 Dec 19;103(51):19326-31. Epub 2006 Dec 6. PMID:17151196^[1]

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

References

↑ Houdusse A, Gaucher JF, Krementsova E, Mui S, Trybus KM, Cohen C. Crystal structure of apo-calmodulin bound to the first two IQ motifs of myosin V reveals essential recognition features. Proc Natl Acad Sci U S A. 2006 Dec 19;103(51):19326-31. Epub 2006 Dec 6. PMID:17151196

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2ix7"

@@ Line 1: / Line 1: @@
-[[Image:2ix7.png|left|200px]]
-{{STRUCTURE_2ix7|  PDB=2ix7  |  SCENE=  }}
+==Structure of apo-calmodulin bound to unconventional myosin V==
+<StructureSection load='2ix7' size='340' side='right'caption='[[2ix7]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[2ix7]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IX7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IX7 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]] 2.5&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CYS:CYSTEINE'>CYS</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=2ix7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ix7 OCA], [https://pdbe.org/2ix7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ix7 RCSB], [https://www.ebi.ac.uk/pdbsum/2ix7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ix7 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/CALM1_MOUSE CALM1_MOUSE] Calmodulin acts as part of a calcium signal transduction pathway by mediating the control of a large number of enzymes, ion channels, aquaporins and other proteins through calcium-binding. Calcium-binding is required for the activation of calmodulin. Among the enzymes to be stimulated by the calmodulin-calcium complex are a number of protein kinases, such as myosin light-chain kinases and calmodulin-dependent protein kinase type II (CaMK2), and phosphatases. Together with CCP110 and centrin, is involved in a genetic pathway that regulates the centrosome cycle and progression through cytokinesis. Is a regulator of voltage-dependent L-type calcium channels. Mediates calcium-dependent inactivation of CACNA1C. Positively regulates calcium-activated potassium channel activity of KCNN2. Forms a potassium channel complex with KCNQ1 and regulates electrophysiological activity of the channel via calcium-binding. Acts as a sensor to modulate the endoplasmic reticulum contacts with other organelles mediated by VMP1:ATP2A2.[UniProtKB:P0DP23]
+== 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/ix/2ix7_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=2ix7 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+A 2.5-A resolution structure of calcium-free calmodulin (CaM) bound to the first two IQ motifs of the murine myosin V heavy chain reveals an unusual CaM conformation. The C-terminal lobe of each CaM adopts a semi-open conformation that grips the first part of the IQ motif (IQxxxR), whereas the N-terminal lobe adopts a closed conformation that interacts more weakly with the second part of the motif (GxxxR). Variable residues in the IQ motif play a critical role in determining the precise structure of the bound CaM, such that even the consensus residues of different motifs show unique interactions with CaM. This complex serves as a model for the lever arm region of many classes of unconventional myosins, as well as other IQ motif-containing proteins such as neuromodulin and IQGAPs.
-===STRUCTURE OF APO-CALMODULIN BOUND TO UNCONVENTIONAL MYOSIN V===
+Crystal structure of apo-calmodulin bound to the first two IQ motifs of myosin V reveals essential recognition features.,Houdusse A, Gaucher JF, Krementsova E, Mui S, Trybus KM, Cohen C Proc Natl Acad Sci U S A. 2006 Dec 19;103(51):19326-31. Epub 2006 Dec 6. PMID:17151196<ref>PMID:17151196</ref>
-{{ABSTRACT_PUBMED_17151196}}
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-==About this Structure==
+<div class="pdbe-citations 2ix7" style="background-color:#fffaf0;"></div>
-[[2ix7]] is a 3 chain structure of [[Calmodulin]] and [[Myosin]] with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IX7 OCA].
 ==See Also==
-*[[Calmodulin|Calmodulin]]
+*[[Calmodulin 3D structures|Calmodulin 3D structures]]
-*[[Myosin|Myosin]]
+*[[Myosin 3D Structures|Myosin 3D Structures]]
+== References ==
-==Reference==
+<references/>
-<ref group="xtra">PMID:017151196</ref><references group="xtra"/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
 [[Category: Mus musculus]]
-[[Category: Cohen, C.]]
+[[Category: Cohen C]]
-[[Category: Gaucher, J F.]]
+[[Category: Gaucher JF]]
-[[Category: Houdusse, A.]]
+[[Category: Houdusse A]]
-[[Category: Krementsova, E.]]
+[[Category: Krementsova E]]
-[[Category: Mui, S.]]
+[[Category: Mui S]]
-[[Category: Trybus, K M.]]
+[[Category: Trybus KM]]
-[[Category: Actin-binding]]
-[[Category: Atp-binding]]
-[[Category: Ca2+ regulation]]
-[[Category: Calmodulin]]
-[[Category: Calmodulin-binding]]
-[[Category: Complex]]
-[[Category: Contractile protein]]
-[[Category: Contractile protein-metal binding complex]]
-[[Category: Contractile protein/metal binding]]
-[[Category: Iq motif]]
-[[Category: Metal binding]]
-[[Category: Methylation]]
-[[Category: Motor protein]]
-[[Category: Myosin]]
-[[Category: Nucleotide- binding]]
-[[Category: Phosphorylation]]

2ix7

From Proteopedia

Current revision

Structure of apo-calmodulin bound to unconventional myosin V

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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