PDBsum entry 4z9s

Cell cycle

PDB id: 4z9s

Contents

Protein chains

75 a.a.

Ligands

MLA ×6

SCN ×9

Waters ×147

PDB id:

4z9s

Name:

Cell cycle

Title:

Non-covalent assembly of monoubiquitin that mimics k11 poly-ubiquitin

Structure:

Ubiquitin-40s ribosomal protein s27a. Chain: a, b, c, d. Fragment: unp residues 1-76. Synonym: ubiquitin carboxyl extension protein 80. Engineered: yes

Source:

Bos taurus. Bovine. Organism_taxid: 9913. Tissue: red blood cells. Gene: ubc. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

2.30Å R-factor: 0.186 R-free: 0.223

Authors:

O.Levin-Kravets,G.Prag

Key ref:

O.Levin-Kravets et al. (2015). Tetrameric Assembly of Monoubiquitin Accurately Mimics the Lys11 Polyubiquitin Chain Structure. Biochemistry, 54, 4704-4710. PubMed id: 26171660 DOI: 10.1021/acs.biochem.5b00498

Date:

11-Apr-15 Release date: 29-Jul-15

Protein chains

P62992  (RS27A_BOVIN) -  Ubiquitin-ribosomal protein eS31 fusion protein from Bos taurus

Seq: 156 a.a.

Struc: 75 a.a.

DOI no: 10.1021/acs.biochem.5b00498

Biochemistry 54:4704-4710 (2015)

PubMed id: 26171660

Tetrameric Assembly of Monoubiquitin Accurately Mimics the Lys11 Polyubiquitin Chain Structure.

O.Levin-Kravets, N.Shohat, G.Prag.

ABSTRACT

Specific lysine residues on the ubiquitin surface were selected during the course of evolution to form different polyubiquitin chain structures that signal diverse cellular processes. A vast number of ubiquitin receptors specifically recognize and decode the signals conferred by these polyubiquitin chains. The mechanisms of formation and the structure of Lys11-linked ubiquitin, which signals for cell-cycle and innate immune control, have been elucidated. Here, we present a new crystal structure of monomeric ubiquitin that accurately mimics one of the structures of Lys11-linked ubiquitin. Analysis of the ubiquitin:ubiquitin interface demonstrates structural fitness and specificity. The interaction is exclusively hydrophilic, leaving the Ile44 hydrophobic patch, a major recognition site for ubiquitin receptors, exposed. These noncovalent ubiquitin:ubiquitin interactions are nearly identical to those reported for Lys11-linked ubiquitin and seem to play a significant role in stabilizing the crystal structure without the isopeptide bond. In vitro cross-linking analysis with wild-type ubiquitin or its mutants partially mimics the interactions in the crystal. We suggest that these interactions may play a biological role in transmitting Lys11-linked ubiquitin chain-type cellular signals.