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| | <StructureSection load='3qrx' size='340' side='right'caption='[[3qrx]], [[Resolution|resolution]] 2.20Å' scene=''> | | <StructureSection load='3qrx' size='340' side='right'caption='[[3qrx]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3qrx]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Chlre Chlre]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QRX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QRX FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3qrx]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Apis_mellifera Apis mellifera] and [https://en.wikipedia.org/wiki/Chlamydomonas_reinhardtii Chlamydomonas reinhardtii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QRX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QRX FirstGlance]. <br> |
| - | </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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">VFL2, CHLREDRAFT_159554 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3055 CHLRE])</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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3qrx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qrx OCA], [https://pdbe.org/3qrx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qrx RCSB], [https://www.ebi.ac.uk/pdbsum/3qrx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qrx ProSAT]</span></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=3qrx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qrx OCA], [https://pdbe.org/3qrx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qrx RCSB], [https://www.ebi.ac.uk/pdbsum/3qrx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qrx ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/MEL_APIME MEL_APIME]] Melittin: Main toxin of bee venom with strong hemolytic activity. Forms a pore in the cell membrane by inserting into lipid bilayers in an alpha-helical conformation and has multiple effects, probably, as a result of its interaction with negatively charged phospholipids. It inhibits well known transport pumps such as the Na(+)-K(+)-ATPase and the H(+)-K(+)-ATPase. It increases the permeability of cell membranes to ions, particularly Na(+) and indirectly Ca(2+), because of the Na(+)-Ca(2+)-exchange. It acts synergistically with phospholipase A2.<ref>PMID:20472009</ref> Melittin-S: 1.4-fold less hemolytic and adopts a less organized secondary structure than melittin.<ref>PMID:20472009</ref>
| + | [https://www.uniprot.org/uniprot/CATR_CHLRE CATR_CHLRE] This calcium-binding protein is found in the basal body complexes (the functional homolog of the centrosome in animal cell). In mitotic cells it is specifically associated with the poles of the mitotic spindles at the sites of the duplicated basal body complexes. |
| - | <div style="background-color:#fffaf0;">
| + | |
| - | == Publication Abstract from PubMed ==
| + | |
| - | Centrin is a calcium binding protein (CaBP) belonging to the EF-hand superfamily. As with other proteins within this family, centrin is a calcium sensor with multiple biological target proteins. We chose to study Chlamydomonas reinhardtii centrin (Crcen) and its interaction with melittin (MLT) as a model for CaBP complexes due to its amphipathic properties. Our goal was to determine the molecular interactions that lead to centrin-MLT complex formation, their relative stability, and the conformational changes associated with the interaction, when compared to the single components. For this, we determined the thermodynamic parameters that define Crcen-MLT complex formation. Two-dimensional infrared (2D IR) correlation spectroscopy were used to study the amide I', I'*, and side chain bands for (13) C-Crcen, MLT, and the (13) C-Crcen-MLT complex. This approach resulted in the determination of MLT's increased helicity, while centrin was stabilized within the complex. Herein we provide the first complete molecular description of centrin-MLT complex formation and the dissociation process. Also, discussed is the first structure of a CaBP-MLT complex by X-ray crystallography, which shows that MLT has a different binding orientation than previously characterized centrin-bound peptides. Finally, all of the experimental results presented herein are consistent with centrin maintaining an extended conformation while interacting with MLT. The molecular implications of these results are: (1) the recognition of hydrophobic contacts as requirements for initial binding, (2) minimum electrostatic interactions within the C-terminal end of the peptide, and (3) van der Waals interactions within MLTs N-terminal end are required for complex formation. Proteins 2011; (c) 2011 Wiley-Liss, Inc.
| + | |
| - | | + | |
| - | The structure, molecular dynamics, and energetics of centrin-melittin complex.,Sosa Ldel V, Alfaro E, Santiago J, Narvaez D, Rosado MC, Rodriguez A, Gomez AM, Schreiter ER, Pastrana-Rios B Proteins. 2011 Nov;79(11):3132-43. doi: 10.1002/prot.23142. Epub 2011 Aug, 30. PMID:21989934<ref>PMID:21989934</ref>
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| - | | + | |
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| + | |
| - | </div>
| + | |
| - | <div class="pdbe-citations 3qrx" style="background-color:#fffaf0;"></div>
| + | |
| - | == References ==
| + | |
| - | <references/>
| + | |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Chlre]] | + | [[Category: Apis mellifera]] |
| | + | [[Category: Chlamydomonas reinhardtii]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Schreiter, E R]] | + | [[Category: Schreiter ER]] |
| - | [[Category: Calcium binding]]
| + | |
| - | [[Category: Calcium-binding]]
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| - | [[Category: Cell division]]
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| - | [[Category: Ef-hand]]
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| - | [[Category: Metal binding protein-toxin complex]]
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