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2lmv

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==Androcam at high calcium with three explicit Ca2+==
==Androcam at high calcium with three explicit Ca2+==
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<StructureSection load='2lmv' size='340' side='right' caption='[[2lmv]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
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<StructureSection load='2lmv' size='340' side='right'caption='[[2lmv]]' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2lmv]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LMV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2LMV FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2lmv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LMV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LMV FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene><br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2lmt|2lmt]], [[2lmu|2lmu]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
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<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">And, androcam, Camr97A, CG17769 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 Drosophila melanogaster])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2lmv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lmv OCA], [https://pdbe.org/2lmv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lmv RCSB], [https://www.ebi.ac.uk/pdbsum/2lmv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lmv ProSAT]</span></td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2lmv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lmv OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2lmv RCSB], [http://www.ebi.ac.uk/pdbsum/2lmv PDBsum]</span></td></tr>
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</table>
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<table>
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== Function ==
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<div style="background-color:#fffaf0;">
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[https://www.uniprot.org/uniprot/CALL_DROME CALL_DROME] May be involved in calcium-mediated signal transduction.<ref>PMID:7980384</ref>
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== Publication Abstract from PubMed ==
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Androcam replaces calmodulin as a tissue-specific myosin VI light chain on the actin cones that mediate D. melanogaster spermatid individualization. We show that the androcam structure and its binding to the myosin VI structural (Insert 2) and regulatory (IQ) light chain sites are distinct from those of calmodulin and provide a basis for specialized myosin VI function. The androcam N lobe noncanonically binds a single Ca(2+) and is locked in a "closed" conformation, causing androcam to contact the Insert 2 site with its C lobe only. Androcam replacing calmodulin at Insert 2 will increase myosin VI lever arm flexibility, which may favor the compact monomeric form of myosin VI that functions on the actin cones by facilitating the collapse of the C-terminal region onto the motor domain. The tethered androcam N lobe could stabilize the monomer through contacts with C-terminal portions of the motor or recruit other components to the actin cones. Androcam binds the IQ site at all calcium levels, constitutively mimicking a conformation adopted by calmodulin only at intermediate calcium levels. Thus, androcam replacing calmodulin at IQ will abolish a Ca(2+)-regulated, calmodulin-mediated myosin VI structural change. We propose that the N lobe prevents androcam from interfering with other calmodulin-mediated Ca(2+) signaling events. We discuss how gene duplication and mutations that selectively stabilize one of the many conformations available to calmodulin support the molecular evolution of structurally and functionally distinct calmodulin-like proteins.
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Structure of androcam supports specialized interactions with myosin VI.,Joshi MK, Moran S, Beckingham KM, Mackenzie KR Proc Natl Acad Sci U S A. 2012 Aug 14;109(33):13290-5. Epub 2012 Jul 31. PMID:22851764<ref>PMID:22851764</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Drosophila melanogaster]]
[[Category: Drosophila melanogaster]]
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[[Category: Beckingham, K M.]]
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[[Category: Large Structures]]
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[[Category: Joshi, M K.]]
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[[Category: Beckingham KM]]
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[[Category: Mackenzie, K R.]]
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[[Category: Joshi MK]]
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[[Category: Moran, S T.]]
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[[Category: Mackenzie KR]]
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[[Category: High calcium]]
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[[Category: Moran ST]]
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[[Category: Metal binding protein]]
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[[Category: Spermatogenesis]]
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Current revision

Androcam at high calcium with three explicit Ca2+

PDB ID 2lmv

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