1c7w
From Proteopedia
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| - | [[Image:1c7w.gif|left|200px]] | ||
| - | + | ==NMR SOLUTION STRUCTURE OF THE CALCIUM-BOUND C-TERMINAL DOMAIN (W81-S161) OF CALCIUM VECTOR PROTEIN FROM AMPHIOXUS== | |
| - | + | <StructureSection load='1c7w' size='340' side='right'caption='[[1c7w]]' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[1c7w]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Branchiostoma_lanceolatum Branchiostoma lanceolatum]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C7W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1C7W FirstGlance]. <br> | |
| - | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1c7w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c7w OCA], [https://pdbe.org/1c7w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1c7w RCSB], [https://www.ebi.ac.uk/pdbsum/1c7w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1c7w ProSAT]</span></td></tr> | |
| - | + | </table> | |
| - | + | == Function == | |
| - | + | [https://www.uniprot.org/uniprot/CAVP_BRALA CAVP_BRALA] The exact function of this protein is not yet known. It interacts with CAVPT, a protein also of unknown function, in a calcium-dependent way. This protein binds two calcium ions. | |
| - | + | == 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/c7/1c7w_consurf.spt"</scriptWhenChecked> | |
| - | == | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1c7w ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
Calcium vector protein (CaVP) from amphioxus is a two-domain, calcium-binding protein (18.3 kDa) of the calmodulin superfamily. Only two of the four EF-hand motifs (sites III and IV) have a significant binding affinity for calcium ions. We determined the solution structure of the domain containing these active sites (C-CaVP: W81-S161), in the Ca(2+)-saturated state, using NMR spectroscopy and restrained molecular dynamics. The tertiary structure is similar to other Ca(2+)-binding domains containing a pair of EF-hand motifs. The apo state has spectroscopic and thermodynamic characteristics of a molten globule, with conserved secondary structure but highly fluctuating tertiary organization. Titration of C-CaVP with Ca(2+) revealed a stepwise ion binding, with a stable equilibrium intermediate in which only site III binds a calcium ion. Despite a highly fluctuating structure of the free site IV, the calcium-bound site III has a persistent structure, with similar secondary elements but different interhelix angle and hydrophobic packing relative to the fully calcium-saturated state. | Calcium vector protein (CaVP) from amphioxus is a two-domain, calcium-binding protein (18.3 kDa) of the calmodulin superfamily. Only two of the four EF-hand motifs (sites III and IV) have a significant binding affinity for calcium ions. We determined the solution structure of the domain containing these active sites (C-CaVP: W81-S161), in the Ca(2+)-saturated state, using NMR spectroscopy and restrained molecular dynamics. The tertiary structure is similar to other Ca(2+)-binding domains containing a pair of EF-hand motifs. The apo state has spectroscopic and thermodynamic characteristics of a molten globule, with conserved secondary structure but highly fluctuating tertiary organization. Titration of C-CaVP with Ca(2+) revealed a stepwise ion binding, with a stable equilibrium intermediate in which only site III binds a calcium ion. Despite a highly fluctuating structure of the free site IV, the calcium-bound site III has a persistent structure, with similar secondary elements but different interhelix angle and hydrophobic packing relative to the fully calcium-saturated state. | ||
| - | + | Sequential calcium binding to the regulatory domain of calcium vector protein reveals functional asymmetry and a novel mode of structural rearrangement.,Theret I, Baladi S, Cox JA, Sakamoto H, Craescu CT Biochemistry. 2000 Jul 11;39(27):7920-6. PMID:10891072<ref>PMID:10891072</ref> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| + | <div class="pdbe-citations 1c7w" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Branchiostoma lanceolatum]] | [[Category: Branchiostoma lanceolatum]] | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: Baladi | + | [[Category: Baladi S]] |
| - | [[Category: Cox | + | [[Category: Cox JA]] |
| - | [[Category: Craescu | + | [[Category: Craescu CT]] |
| - | [[Category: Sakamoto | + | [[Category: Sakamoto H]] |
| - | [[Category: Theret | + | [[Category: Theret I]] |
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Current revision
NMR SOLUTION STRUCTURE OF THE CALCIUM-BOUND C-TERMINAL DOMAIN (W81-S161) OF CALCIUM VECTOR PROTEIN FROM AMPHIOXUS
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