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| | <StructureSection load='5d43' size='340' side='right'caption='[[5d43]], [[Resolution|resolution]] 2.82Å' scene=''> | | <StructureSection load='5d43' size='340' side='right'caption='[[5d43]], [[Resolution|resolution]] 2.82Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5d43]] is a 2 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=5D43 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5D43 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5d43]] is a 2 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=5D43 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5D43 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | + | </td></tr><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> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Cetn1, Calt ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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=5d43 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5d43 OCA], [https://pdbe.org/5d43 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5d43 RCSB], [https://www.ebi.ac.uk/pdbsum/5d43 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5d43 ProSAT]</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=5d43 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5d43 OCA], [http://pdbe.org/5d43 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5d43 RCSB], [http://www.ebi.ac.uk/pdbsum/5d43 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5d43 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CETN1_MOUSE CETN1_MOUSE]] Plays a fundamental role in microtubule-organizing center structure and function. | + | [https://www.uniprot.org/uniprot/CETN1_MOUSE CETN1_MOUSE] Plays a fundamental role in microtubule-organizing center structure and function. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lk3 transgenic mice]] | + | [[Category: Mus musculus]] |
| - | [[Category: Kim, D S]] | + | [[Category: Kim DS]] |
| - | [[Category: Kim, S Y]] | + | [[Category: Kim SY]] |
| - | [[Category: Park, J H]] | + | [[Category: Park JH]] |
| - | [[Category: Calcium-binding protein]]
| + | |
| - | [[Category: Centrin]]
| + | |
| - | [[Category: Ef-hand motif]]
| + | |
| - | [[Category: Metal binding protein]]
| + | |
| Structural highlights
Function
CETN1_MOUSE Plays a fundamental role in microtubule-organizing center structure and function.
Publication Abstract from PubMed
Mus musculus centrin 1 (MmCen1) is located at the cilium of photoreceptor cells connecting the outer segment through signal transduction components to the metabolically active inner segment. In the cilium, MmCen1 is involved in the translocation of transducin between compartments as a result of photoreceptor activation. In this study, we report the crystal structure of wild-type MmCen1 and its Ca2+-binding properties using structure-based mutagenesis. The crystal structure exhibits three structural features, i.e. four Ca2+ equally occupied at each EF-hand motif, structural changes accompanying helix motion at the N- and C-lobes, and adoption of N-C type dimerization when Ca2+ binds to EF-hand I and II in the N-lobe. The presence of MmCen1 dimers was confirmed in solution by native PAGE. Isothermal titration calorimetry data showed sequential binding of Ca2+ at four independent sites. Mutations S45A and D49A in EF-hand I alone disrupted the Ca2+-binding property of the wild-type protein. Based on the crystal structure of MmCen1, we suggest that a dimerization mode between the N- and C-lobes may be required by Ca2+ binding at the N-lobe.
Crystal Structure of Wild-Type Centrin 1 from Mus musculus Occupied by Ca2.,Kim SY, Kim DS, Hong JE, Park JH Biochemistry (Mosc). 2017 Oct;82(10):1129-1139. doi: 10.1134/S0006297917100054. PMID:29037133[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kim SY, Kim DS, Hong JE, Park JH. Crystal Structure of Wild-Type Centrin 1 from Mus musculus Occupied by Ca2. Biochemistry (Mosc). 2017 Oct;82(10):1129-1139. doi: 10.1134/S0006297917100054. PMID:29037133 doi:http://dx.doi.org/10.1134/S0006297917100054
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