PDBsum entry 5tuc

Hydrolase activator

PDB id: 5tuc

Contents

Protein chains

331 a.a.

315 a.a.

Waters ×154

PDB id:

5tuc

Name:

Hydrolase activator

Title:

Crystal structure of the sus tbc1d15 gap domain

Structure:

Sus tbc1d15 gap domain. Chain: a, b. Fragment: unp residues 270-617. Engineered: yes

Source:

Sus scrofa. Pig. Organism_taxid: 9823. Gene: tbc1d15. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

2.50Å R-factor: 0.217 R-free: 0.253

Authors:

Y.-N.Chen,W.Wang,D.Cheng,Y.Ge,X.Gu,X.E.Zhou,F.Ye,H.E.Xu,Z.Lv

Key ref:

Y.N.Chen et al. (2017). Crystal structure of TBC1D15 GTPase-activating protein (GAP) domain and its activity on Rab GTPases. Protein Sci, 26, 834-846. PubMed id: 28168758 DOI: 10.1002/pro.3132

Date:

05-Nov-16 Release date: 22-Feb-17

Protein chain

F1SH24  (F1SH24_PIG) -  TBC1 domain family member 15 from Sus scrofa

Seq: 649 a.a.

Struc: 331 a.a.

Protein chain

F1SH24  (F1SH24_PIG) -  TBC1 domain family member 15 from Sus scrofa

Seq: 649 a.a.

Struc: 315 a.a.

DOI no: 10.1002/pro.3132

Protein Sci 26:834-846 (2017)

PubMed id: 28168758

Crystal structure of TBC1D15 GTPase-activating protein (GAP) domain and its activity on Rab GTPases.

Y.N.Chen, X.Gu, X.E.Zhou, W.Wang, D.Cheng, Y.Ge, F.Ye, H.E.Xu, Z.Lv.

ABSTRACT

TBC1D15 belongs to the TBC (Tre-2/Bub2/Cdc16) domain family and functions as a GTPase-activating protein (GAP) for Rab GTPases. So far, the structure of TBC1D15 or the TBC1D15·Rab complex has not been determined, thus, its catalytic mechanism on Rab GTPases is still unclear. In this study, we solved the crystal structures of the Shark and Sus TBC1D15 GAP domains, to 2.8 Å and 2.5 Å resolution, respectively. Shark-TBC1D15 and Sus-TBC1D15 belong to the same subfamily of TBC domain-containing proteins, and their GAP-domain structures are highly similar. This demonstrates the evolutionary conservation of the TBC1D15 protein family. Meanwhile, the newly determined crystal structures display new variations compared to the structures of yeast Gyp1p Rab GAP domain and TBC1D1. GAP assays show that Shark and Sus GAPs both have higher catalytic activity on Rab11a·GTP than Rab7a·GTP, which differs from the previous study. We also demonstrated the importance of arginine and glutamine on the catalytic sites of Shark GAP and Sus GAP. When arginine and glutamine are changed to alanine or lysine, the activities of Shark GAP and Sus GAP are lost.