PDBsum entry 3ons

Signaling protein

PDB id: 3ons

Contents

Protein chain

72 a.a. *

Waters ×91

* Residue conservation analysis

PDB id:

3ons

Name:

Signaling protein

Title:

Crystal structure of human ubiquitin in a new crystal form

Structure:

Ubiquitin. Chain: a. Engineered: yes

Source:

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

Resolution:

1.80Å R-factor: 0.183 R-free: 0.211

Authors:

G.A.Amodeo,K.Y.Huang,A.E.Mcdermott,L.Tong

Key ref:

K.Y.Huang et al. (2011). The structure of human ubiquitin in 2-methyl-2,4-pentanediol: a new conformational switch. Protein Sci, 20, 630-639. PubMed id: 21432937

Date:

30-Aug-10 Release date: 23-Feb-11

Protein chain

P0CG48  (UBC_HUMAN) -  Polyubiquitin-C from Homo sapiens

Seq: 685 a.a.

Struc: 72 a.a.

Enzyme reactions

• Enzyme class: E.C.?

Protein Sci 20:630-639 (2011)

PubMed id: 21432937

The structure of human ubiquitin in 2-methyl-2,4-pentanediol: a new conformational switch.

K.Y.Huang, G.A.Amodeo, L.Tong, A.McDermott.

ABSTRACT

A new crystal structure of human ubiquitin is reported at 1.8 Å resolution. Compared with the other known crystal structure or the solution NMR structure of monomeric human ubiquitin, this new structure is similar in its overall fold but differs with respect to the conformation of the backbone in a surface-exposed region. The conformation reported here resembles conformations previously seen in complex with deubiquinating enzymes, wherein the Asp52/Gly53 main chain and Glu24 side chain move. This movement exposes the backbone carbonyl of Asp52 to the exterior of the molecule, making it possible to engage in hydrogen-bond contacts with neighboring molecules, rather than in an internal hydrogen bond with the backbone of Glu24. This particular crystal form of ubiquitin has been used in a large number of solid state NMR studies. The structure described here elucidates the origin of many of the chemical shift differences comparing solution and solid state studies.