PDBsum entry 2m7q

Metal binding protein

PDB id: 2m7q

Contents

Protein chain

69 a.a.

Metals

_ZN ×2

PDB id:

2m7q

Name:

Metal binding protein

Title:

Solution structure of tax1bp1 ubz1+2

Structure:

Tax1-binding protein 1. Chain: a. Fragment: unp residues 725-789. Synonym: traf6-binding protein. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: tax1bp1. Expressed in: escherichia coli. Expression_system_taxid: 562.

NMR struc:

20 models

Authors:

M.A.Ceregido,M.Spinola Amilibia,L.Buts,J.Bravo,N.A.J.Van Nuland

Key ref:

M.A.Ceregido et al. (2014). The structure of TAX1BP1 UBZ1+2 provides insight into target specificity and adaptability. J Mol Biol, 426, 674-690. PubMed id: 24239949 DOI: 10.1016/j.jmb.2013.11.006

Date:

29-Apr-13 Release date: 04-Dec-13

Protein chain

Q86VP1  (TAXB1_HUMAN) -  Tax1-binding protein 1 from Homo sapiens

Seq: 789 a.a.

Struc: 69 a.a.*

* PDB and UniProt seqs differ at 4 residue positions (black crosses)

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1016/j.jmb.2013.11.006

J Mol Biol 426:674-690 (2014)

PubMed id: 24239949

The structure of TAX1BP1 UBZ1+2 provides insight into target specificity and adaptability.

M.A.Ceregido, M.Spínola Amilibia, L.Buts, J.Rivera-Torres, A.Garcia-Pino, J.Bravo, N.A.van Nuland.

ABSTRACT

TAX1BP1 is a novel ubiquitin-binding adaptor protein involved in the negative regulation of the NF-kappaB transcription factor, which is a key player in inflammatory responses, immunity and tumorigenesis. TAX1BP1 recruits A20 to the ubiquitinated signaling proteins TRAF6 and RIP1, leading to their A20-mediated deubiquitination and the disruption of IL-1-induced and TNF-induced NF-kappaB signaling, respectively. The two zinc fingers localized at its C-terminus function as novel ubiquitin-binding domains (UBZ, ubiquitin-binding zinc finger). Here we present for the first time both the solution and crystal structures of two classical UBZ domains in tandem within the human TAX1BP1. The relative orientation of the two domains is slightly different in the X-ray structure with respect to the NMR structure, indicating some degree of conformational flexibility, which is rationalized by NMR relaxation data. The observed degree of flexibility and stability between the two UBZ domains might have consequences on the recognition mechanism of interacting partners.