PDBsum entry 2luh

Protein transport, endocytosis

PDB id: 2luh

Contents

Protein chains

167 a.a.

59 a.a.

PDB id:

2luh

Name:

Protein transport, endocytosis

Title:

Nmr structure of the vta1-vps60 complex

Structure:

Vacuolar protein sorting-associated protein vta1. Chain: a. Synonym: vps20-associated protein 1. Engineered: yes. Vacuolar protein-sorting-associated protein 60. Chain: b. Synonym: charged multivesicular body protein 5. Engineered: yes

Source:

Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 559292. Strain: atcc 204508 / s288c. Gene: vta1, ylr181c. Expressed in: escherichia coli. Expression_system_taxid: 562. Gene: vps60, chm5, mos10, ydr486c.

NMR struc:

20 models

Authors:

Z.Yang,C.Vild,J.Ju,X.Zhang,J.Liu,J.Shen,B.Zhao,W.Lan,F.Gong,M.Liu, C.Cao,Z.Xu

Key ref:

Z.Yang et al. (2012). Structural basis of molecular recognition between ESCRT-III-like protein Vps60 and AAA-ATPase regulator Vta1 in the multivesicular body pathway. J Biol Chem, 287, 43899-43908. PubMed id: 23105107

Date:

13-Jun-12 Release date: 07-Nov-12

Protein chain

Q06263  (VTA1_YEAST) -  Vacuolar protein sorting-associated protein VTA1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: 330 a.a.

Struc: 167 a.a.

Protein chain

Q03390  (VPS60_YEAST) -  Vacuolar protein-sorting-associated protein 60 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: 229 a.a.

Struc: 59 a.a.

Enzyme reactions

• Enzyme class: Chains A, B: E.C.?

J Biol Chem 287:43899-43908 (2012)

PubMed id: 23105107

Structural basis of molecular recognition between ESCRT-III-like protein Vps60 and AAA-ATPase regulator Vta1 in the multivesicular body pathway.

Z.Yang, C.Vild, J.Ju, X.Zhang, J.Liu, J.Shen, B.Zhao, W.Lan, F.Gong, M.Liu, C.Cao, Z.Xu.

ABSTRACT

The AAA-ATPase Vps4 is critical for function of the multivesicular body sorting pathway, which impacts cellular phenomena ranging from receptor down-regulation to viral budding to cytokinesis. Vps4 activity is stimulated by the interaction between Vta1 and Vps60, but the structural basis for this interaction is unclear. The fragment Vps60(128-186) was reported to display the full activity of Vps60. Vta1 interacts with Vps60 using its N-terminal domain (Vta1NTD). In this work, the structure of Vps60(128-186) in complex with Vta1NTD was determined using NMR techniques, demonstrating a novel recognition mode of the microtubule-interacting and transport (MIT) domain in which Vps60(128-186) interacts with Vta1NTD through helices α4' and α5', extending over Vta1NTD MIT2 domain helices 1-3. The Vps60 binding does not result in Vta1 conformational changes, further revealing the fact that Vps4 ATPase is enhanced by the interaction between Vta1 and Vps60 in an unanticipated manner.