PDBsum entry 2f0r

Unknown function

PDB id: 2f0r

Contents

Protein chain

143 a.a. *

Ligands

SO4 ×2

Waters ×241

* Residue conservation analysis

PDB id:

2f0r

Name:

Unknown function

Title:

Crystallographic structure of human tsg101 uev domain

Structure:

Tumor susceptibility gene 101 protein. Chain: a, b. Synonym: tsg101(uev) domain. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: tsg101. Expressed in: escherichia coli. Expression_system_taxid: 562

Biol. unit:

Dimer (from PQS)

Resolution:

2.26Å R-factor: 0.191 R-free: 0.243

Authors:

A.Camara-Artigas,I.Luque,A.Palencia,J.C.Martinez,P.L.Mateo

Key ref:

A.Palencia et al. (2006). Structure of human TSG101 UEV domain. Acta Crystallogr D Biol Crystallogr, 62, 458-464. PubMed id: 16552148 DOI: 10.1107/S0907444906005221

Date:

13-Nov-05 Release date: 28-Mar-06

Protein chains

Q99816  (TS101_HUMAN) -  Tumor susceptibility gene 101 protein from Homo sapiens

Seq: 390 a.a.

Struc: 143 a.a.

DOI no: 10.1107/S0907444906005221

Acta Crystallogr D Biol Crystallogr 62:458-464 (2006)

PubMed id: 16552148

Structure of human TSG101 UEV domain.

A.Palencia, J.C.Martinez, P.L.Mateo, I.Luque, A.Camara-Artigas.

ABSTRACT

The UEV domain of the TSG101 protein functions in the vacuolar protein-sorting pathway and in the budding process of HIV-1 and other retroviruses by recognizing ubiquitin in proteins tagged for degradation and short sequences in viral proteins containing an essential and well conserved PTAP motif, respectively. A deep understanding of these interactions is key to the rational design of much-needed novel antivirals. Here, the crystal structure of the TSG101 UEV domain (TSG101-UEV) is presented. TSG101-UEV was crystallized in the presence of PEG 4000 and ammonium sulfate. Under these conditions, crystals were obtained in space group R3, with unit-cell parameters a = b = 97.9, c = 110.6 A, alpha = beta = 90, gamma = 120 degrees . Phases were solved by molecular replacement and the crystal structure of TSG101-UEV was refined to an R factor of 18.8% at 2.2 A resolution. A comparison between the crystal structure and previously reported NMR structures has revealed significant differences in the conformation of one of the loops implicated in ubiquitin recognition. Also, the resulting structure has provided information about the presence of water molecules at the binding interface that could be of relevance for peptide recognition.

Selected figure(s)

Figure 2.
Ribbon representation of the crystal structure of the human TSG101 UEV domain. [beta] -Strands are coloured yellow and labelled S1-S5 and [alpha] -helices are coloured red and labelled H1-H3. Loops important for ubiquitin recognition are labelled `lip' and `tongue'.

The above figure is reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (2006, 62, 458-464) copyright 2006.

Figure was selected by the author.