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| | ==NMR solution structure of N-terminal domain of (Y81F)-EhCaBP1== | | ==NMR solution structure of N-terminal domain of (Y81F)-EhCaBP1== |
| - | <StructureSection load='2m7k' size='340' side='right'caption='[[2m7k]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | + | <StructureSection load='2m7k' size='340' side='right'caption='[[2m7k]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2m7k]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Enthi Enthi]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2M7K OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2M7K FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2m7k]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Entamoeba_histolytica Entamoeba histolytica]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2M7K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2M7K FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2m7k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2m7k OCA], [http://pdbe.org/2m7k PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2m7k RCSB], [http://www.ebi.ac.uk/pdbsum/2m7k PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2m7k ProSAT]</span></td></tr> | + | </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=2m7k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2m7k OCA], [https://pdbe.org/2m7k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2m7k RCSB], [https://www.ebi.ac.uk/pdbsum/2m7k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2m7k ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CALBP_ENTHI CALBP_ENTHI]] Could play a role in the transduction of secondary messages on binding of calcium. | + | [https://www.uniprot.org/uniprot/CALBP_ENTHI CALBP_ENTHI] Could play a role in the transduction of secondary messages on binding of calcium. |
| - | <div style="background-color:#fffaf0;">
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| - | == Publication Abstract from PubMed ==
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| - | EhCaBP1, one of the calcium binding proteins from E. histolytica, is a two-domain EF-hand protein. The two domains of EhCaBP1 are structurally and functionally different from each other. However, both the domains are required for structural stability and full range of functional diversity. Analysis of sequence and structure of EhCaBP1 and other CaBPs indicates that the C-terminal domain of EhCaBP1 possesses unique structure compared to other family members. This had been attributed to the absence of Phe-Phe interaction between highly conserved Phe residues at -4th position in the EF-hand III (F[-4]; Y81) and that at the 13th position in the EF-hand IV (F[+13]; F129) of the C-terminal domain. Against this backdrop, we mutated the Tyr residue at -4th position of EF III to Phe residue (Y81F), to bring in Phe-Phe interaction and to understand the nature of structural and functional changes in the protein by NMR spectroscopy, molecular dynamics (MD) simulation, isothermal titration calorimetry (ITC) and biological assays, such as imaging and actin binding. The Y81F mutation in EhCaBP1 resulted in a more compact structure for the C-terminal domain of the mutant as in the case of calmodulin and troponin C. The compact structure is favoured by the presence of pi-pi interaction between F81 and F129 along with several hydrophobic interactions of F81, which are not seen in the wild type protein. Further, the biological assays reveal preferential membrane localization of the mutant, loss of its colocalization with actin in the phagocytic cups while retaining its ability to binding G- and F-actin.
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| - | Functional manipulation of a calcium binding protein from E. histolytica guided by paramagnetic NMR.,Rout AK, Patel S, Gupta S, Shukla M, Saraswathi D, Bhattacharya A, Chary KV J Biol Chem. 2013 Jun 19. PMID:23782698<ref>PMID:23782698</ref>
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| - | </div>
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| - | <div class="pdbe-citations 2m7k" style="background-color:#fffaf0;"></div>
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| - | == References ==
| + | |
| - | <references/>
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Enthi]] | + | [[Category: Entamoeba histolytica]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Bhattacharya, A]] | + | [[Category: Bhattacharya A]] |
| - | [[Category: Chary, K V]] | + | [[Category: Chary KV]] |
| - | [[Category: Patel, S]] | + | [[Category: Patel S]] |
| - | [[Category: Rout, A K]] | + | [[Category: Rout AK]] |
| - | [[Category: Metal binding protein]]
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