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| <StructureSection load='6ado' size='340' side='right'caption='[[6ado]], [[Resolution|resolution]] 2.50Å' scene=''> | | <StructureSection load='6ado' size='340' side='right'caption='[[6ado]], [[Resolution|resolution]] 2.50Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[6ado]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Leido Leido]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ADO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6ADO FirstGlance]. <br> | | <table><tr><td colspan='2'>[[6ado]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Leishmania_donovani Leishmania donovani]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ADO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6ADO FirstGlance]. <br> |
| </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5cx2|5cx2]]</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]] 2.502Å</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=6ado FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ado OCA], [http://pdbe.org/6ado PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ado RCSB], [http://www.ebi.ac.uk/pdbsum/6ado PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ado 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=6ado FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ado OCA], [https://pdbe.org/6ado PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ado RCSB], [https://www.ebi.ac.uk/pdbsum/6ado PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ado ProSAT]</span></td></tr> |
| </table> | | </table> |
| <div style="background-color:#fffaf0;">
| | == Function == |
| == Publication Abstract from PubMed == | | [https://www.uniprot.org/uniprot/Q3T1U8_LEIDO Q3T1U8_LEIDO] |
| Protein-protein interactions of cellular importance are mediated by coiled coils (CCs), the ubiquitous structural motif formed by the association of two or more alpha-helices in a knobs into holes manner. Coronins, actin-associated multi-functional proteins that possess distinct cytoskeleton-dependent and independent functions, oligomerize through their C-terminal CC domain. The structure of the L. donovani coronin CC domain (LdCoroCC; PDB ID 5CX2) revealed, in addition to a novel topology and architecture, an inherent asymmetry, with one of the helices of the 4-helix bundle axially shifted ( approximately 2 turns). The structural analysis identified that steric hindrance by Ile 486, Leu 493 and Met 500 as the cause for this asymmetry. To experimentally validate this hypothesis and to better understand the sequence-structure relationship in CCs, these amino acids have been mutated (I486A, L493A, M500V and the double mutant I486A-L493A) and characterized. Thermal CD studies suggest that the I486A and M500V mutants have comparable Tm values to LdCoroCC, while the other mutants have lower melting temperatures. The mutant crystal structures (I486A, M500V and the double mutant) retain the 'ade' core packing as LdcoroCC. While the M500V structure is similar to LdCoroCC, the I486A and the I486A-L493A structures show an asymmetry to symmetry transition. This study reveals crucial role of residues at position 'a' in coiled-coil domain play an important role in stabilizing the asymmetry in LdCoroCC, which might be necessary pursue specific biological function(s) inside the Leishmania.
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| Molecular and Structural analysis of a mechanical transition of helices in the L. donovani coronin coiled-coil domain.,Shrimant Karade S, Ansari A, Kumar Srivastava V, Ranjan Nayak A, Venkatesh Pratap J Int J Biol Macromol. 2019 Nov 25. pii: S0141-8130(19)31056-6. doi:, 10.1016/j.ijbiomac.2019.09.138. PMID:31778699<ref>PMID:31778699</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 6ado" style="background-color:#fffaf0;"></div>
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| == References ==
| |
| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: Leido]] | | [[Category: Leishmania donovani]] |
| [[Category: Ansari, A]] | | [[Category: Ansari A]] |
| [[Category: Karade, S S]] | | [[Category: Karade SS]] |
| [[Category: Pratap, J V]] | | [[Category: Pratap JV]] |
| [[Category: Mutant of actin-associated protein coronin of leishmania donovani]]
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| [[Category: Structural protein]]
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