4CKM
Structure of the N-terminal domain of Leishmania SAS-6
Summary for 4CKM
| Entry DOI | 10.2210/pdb4ckm/pdb |
| Related | 4CKN 4CKP |
| Descriptor | SAS-6, MAGNESIUM ION, GLYCEROL, ... (4 entities in total) |
| Functional Keywords | structural protein, basal body, centriole, cartwheel, trypanosomatids |
| Biological source | LEISHMANIA MAJOR |
| Total number of polymer chains | 3 |
| Total formula weight | 59181.68 |
| Authors | van Breugel, M. (deposition date: 2014-01-07, release date: 2014-03-05, Last modification date: 2024-05-08) |
| Primary citation | van Breugel, M.,Wilcken, R.,McLaughlin, S.H.,Rutherford, T.J.,Johnson, C.M. Structure of the SAS-6 cartwheel hub from Leishmania major. Elife, 3:e01812-e01812, 2014 Cited by PubMed Abstract: Centrioles are cylindrical cell organelles with a ninefold symmetric peripheral microtubule array that is essential to template cilia and flagella. They are built around a central cartwheel assembly that is organized through homo-oligomerization of the centriolar protein SAS-6, but whether SAS-6 self-assembly can dictate cartwheel and thereby centriole symmetry is unclear. Here we show that Leishmania major SAS-6 crystallizes as a 9-fold symmetric cartwheel and provide the X-ray structure of this assembly at a resolution of 3.5 Å. We furthermore demonstrate that oligomerization of Leishmania SAS-6 can be inhibited by a small molecule in vitro and provide indications for its binding site. Our results firmly establish that SAS-6 can impose cartwheel symmetry on its own and indicate how this process might occur mechanistically in vivo. Importantly, our data also provide a proof-of-principle that inhibition of SAS-6 oligomerization by small molecules is feasible. DOI: http://dx.doi.org/10.7554/eLife.01812.001. PubMed: 24596152DOI: 10.7554/eLife.01812 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.15 Å) |
Structure validation
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