2YC4

Intraflagellar Transport Complex 25-27 from Chlamydomonas

Summary for 2YC4

• Entry DOI: 10.2210/pdb2yc4/pdb
• Related: 2YC2
• Descriptor: INTRAFLAGELLAR TRANSPORT PROTEIN 25, SMALL RAB-RELATED GTPASE, CALCIUM ION, ... (6 entities in total)
• Functional Keywords: transport protein, cilium, ift complex
• Biological source: CHLAMYDOMONAS REINHARDTII (GREEN ALGAE); More
• Total number of polymer chains: 4
• Total formula weight: 77662.09

Authors

Bhogaraju, S.,Taschner, M.,Lorentzen, E. (deposition date: 2011-03-11, release date: 2011-03-23, Last modification date: 2023-12-20)

Primary citation

Bhogaraju, S.,Taschner, M.,Morawetz, M.,Basquin, C.,Lorentzen, E.
Crystal Structure of the Intraflagellar Transport Complex 25/27.
Embo J., 30:1907-, 2011

PubMed Abstract: The cilium is an important organelle that is found on many eukaryotic cells, where it serves essential functions in motility, sensory reception and signalling. Intraflagellar transport (IFT) is a vital process for the formation and maintenance of cilia. We have determined the crystal structure of Chlamydomonas reinhardtii IFT25/27, an IFT sub-complex, at 2.6 Å resolution. IFT25 and IFT27 interact via a conserved interface that we verify biochemically using structure-guided mutagenesis. IFT27 displays the fold of Rab-like small guanosine triphosphate hydrolases (GTPases), binds GTP and GDP with micromolar affinity and has very low intrinsic GTPase activity, suggesting that it likely requires a GTPase-activating protein (GAP) for robust GTP turnover. A patch of conserved surface residues contributed by both IFT25 and IFT27 is found adjacent to the GTP-binding site and could mediate the binding to other IFT proteins as well as to a potential GAP. These results provide the first step towards a high-resolution structural understanding of the IFT complex.

PubMed: 21505417
DOI: 10.1038/EMBOJ.2011.110

Experimental method

X-RAY DIFFRACTION (2.8 Å)