PDBsum entry 4p17

Unknown function

PDB id: 4p17

Contents

Protein chains

288 a.a.

Waters ×768

PDB id:

4p17

Name:

Unknown function

Title:

Crystal structure of the chlamydomonas flagellar rabgap tbc domain.

Structure:

Rabgap/tbc protein. Chain: a, b. Fragment: unp residues 1-309. Engineered: yes

Source:

Chlamydomonas reinhardtii. Organism_taxid: 3055. Gene: chlredraft_195581. Expressed in: escherichia coli. Expression_system_taxid: 668369.

Resolution:

1.79Å R-factor: 0.197 R-free: 0.260

Authors:

S.Bhogaraju,E.Lorentzen

Key ref:

S.Bhogaraju and E.Lorentzen (2014). Crystal structure of a Chlamydomonas reinhardtii flagellar RabGAP TBC-domain at 1.8 Å resolution. Proteins, 82, 2282-2287. PubMed id: 24810373 DOI: 10.1002/prot.24597

Date:

25-Feb-14 Release date: 30-Apr-14

Protein chains

A8JCA4  (A8JCA4_CHLRE) -

DOI no: 10.1002/prot.24597

Proteins 82:2282-2287 (2014)

PubMed id: 24810373

Crystal structure of a Chlamydomonas reinhardtii flagellar RabGAP TBC-domain at 1.8 Å resolution.

S.Bhogaraju, E.Lorentzen.

ABSTRACT

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; 82:2282-2287. © 2014 Wiley Periodicals, Inc.