4p17

Crystal structure of the Chlamydomonas flagellar RabGAP TBC domain.

spinqualitylabelsall models 4p17, resolution 1.79Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4p17 is a 2 chain structure with sequence from Chlre. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Gene: CHLREDRAFT_195581 (CHLRE) Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed Rab GTPases play a crucial role in the regulation of many intracellular membrane trafficking pathways including endocytosis and ciliogenesis. Rab GTPase activating proteins (RabGAPs) increase the GTP hydrolysis rate of Rab GTPases and turn them into guanine nucleotide diphosphate (GDP) bound inactive form. Here, we determined the crystal structure of the putative catalytic domain of a RabGAP (which we name CrfRabGAP) that is found in the flagellar proteome of the unicellular green alga Chlamydomonas reinhardtii. BLAST searches revealed potential human orthologues of CrfRabGAP as TBC1D3 and TBC1D26. Sequence and structural comparison with other canonical RabGAPs revealed that the CrfRabGAP does not contain the canonical catalytic residues required for the activation of Rab GTPases. The function of noncanonical RabGAPs-like CrfRabGAP might be to serve as Rab effectors rather than activators.Proteins 2014;. (c) 2014 Wiley Periodicals, Inc. Crystal structure of a Chlamydomonas reinhardtii flagellar RabGAP TBC-domain at 1.8 A resolution.,Bhogaraju S, Lorentzen E Proteins. 2014 May 9. doi: 10.1002/prot.24597. PMID:24810373 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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