PDBsum entry 4xok

Signaling protein

PDB id: 4xok

Contents

Protein chains

70 a.a.

Metals

_ZN ×6

Waters ×82

PDB id:

4xok

Name:

Signaling protein

Title:

Observing the overall rocking motion of a protein in a crystal.

Structure:

Ubiquitin. Chain: a, b, c. Synonym: polyubiquitin-c. Engineered: yes

Source:

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

Resolution:

2.20Å R-factor: 0.304 R-free: 0.324

Authors:

N.Coquelle,P.Ma,P.Schanda,J.P.Colletier

Key ref:

P.Ma et al. (2015). Observing the overall rocking motion of a protein in a crystal. Nat Commun, 6, 8361. PubMed id: 26436197 DOI: 10.1038/ncomms9361

Date:

16-Jan-15 Release date: 14-Oct-15

Protein chains

P0CG48  (UBC_HUMAN) -  Polyubiquitin-C from Homo sapiens

Seq: 685 a.a.

Struc: 70 a.a.

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1038/ncomms9361

Nat Commun 6:8361 (2015)

PubMed id: 26436197

Observing the overall rocking motion of a protein in a crystal.

P.Ma, Y.Xue, N.Coquelle, J.D.Haller, T.Yuwen, I.Ayala, O.Mikhailovskii, D.Willbold, J.P.Colletier, N.R.Skrynnikov, P.Schanda.

ABSTRACT

The large majority of three-dimensional structures of biological macromolecules have been determined by X-ray diffraction of crystalline samples. High-resolution structure determination crucially depends on the homogeneity of the protein crystal. Overall 'rocking' motion of molecules in the crystal is expected to influence diffraction quality, and such motion may therefore affect the process of solving crystal structures. Yet, so far overall molecular motion has not directly been observed in protein crystals, and the timescale of such dynamics remains unclear. Here we use solid-state NMR, X-ray diffraction methods and μs-long molecular dynamics simulations to directly characterize the rigid-body motion of a protein in different crystal forms. For ubiquitin crystals investigated in this study we determine the range of possible correlation times of rocking motion, 0.1-100 μs. The amplitude of rocking varies from one crystal form to another and is correlated with the resolution obtainable in X-ray diffraction experiments.