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: @@
 ==Structure of apo-calmodulin bound to unconventional myosin V==
-<StructureSection load='2ix7' size='340' side='right' caption='[[2ix7]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
+<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 [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2IX7 FirstGlance]. <br>
+<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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CYS:CYSTEINE'>CYS</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
+</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='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=2ix7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ix7 OCA], [http://pdbe.org/2ix7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ix7 RCSB], [http://www.ebi.ac.uk/pdbsum/2ix7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2ix7 ProSAT]</span></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 ==
-[[http://www.uniprot.org/uniprot/MYO5A_MOUSE MYO5A_MOUSE]] Processive actin-based motor that can move in large steps approximating the 36-nm pseudo-repeat of the actin filament. Involved in melanosome transport. Also mediates the transport of vesicles to the plasma membrane. May also be required for some polarization process involved in dendrite formation.<ref>PMID:22908308</ref>
+[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]]
@@ Line 14: / Line 15: @@
   <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/initialview01.spt</scriptWhenUnchecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
@@ Line 30: / Line 31: @@
 ==See Also==
-*[[Calmodulin|Calmodulin]]
+*[[Calmodulin 3D structures|Calmodulin 3D structures]]
-*[[Myosin|Myosin]]
+*[[Myosin 3D Structures|Myosin 3D Structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Lk3 transgenic mice]]
+[[Category: Large Structures]]
-[[Category: Cohen, C]]
+[[Category: Mus musculus]]
-[[Category: Gaucher, J F]]
+[[Category: Cohen C]]
-[[Category: Houdusse, A]]
+[[Category: Gaucher JF]]
-[[Category: Krementsova, E]]
+[[Category: Houdusse A]]
-[[Category: Mui, S]]
+[[Category: Krementsova E]]
-[[Category: Trybus, K M]]
+[[Category: Mui S]]
-[[Category: Acetylation]]
+[[Category: Trybus KM]]
-[[Category: Actin-binding]]
-[[Category: Atp-binding]]
-[[Category: Ca2+ regulation]]
-[[Category: Calcium]]
-[[Category: Calmodulin]]
-[[Category: Calmodulin-binding]]
-[[Category: Coiled coil]]
-[[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]]
-[[Category: Ubl conjugation]]

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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