PDBsum entry: 2gzu

Transcription regulator

PDB id: 2gzu

Contents

Protein chains

66 a.a. *

* Residue conservation analysis

PDB id:

2gzu

Name:

Transcription regulator

Title:

High-resolution structure determination of the cylr2 homodimer using intermonomer distances from paramagnetic relaxation enhancement and nmr dipolar couplings

Structure:

Cytolysin regulator 2. Chain: a, b. Synonym: cylr2. Engineered: yes

Source:

Enterococcus faecalis. Organism_taxid: 1351. Gene: cylr2. Expressed in: escherichia coli. Expression_system_taxid: 562

NMR struc:

15 models

Authors:

S.Rumpel,S.Becker,M.Zweckstetter

Key ref:

S.Rumpel et al. (2008). High-resolution structure determination of the CylR2 homodimer using paramagnetic relaxation enhancement and structure-based prediction of molecular alignment. J Biomol Nmr, 40, 1. PubMed id: 18026911 DOI: 10.1007/s10858-007-9204-4

Date:

12-May-06 Release date: 24-Apr-07

Protein chains

Q8VL32  (Q8VL32_ENTFA) -  CylR2

Seq: 66 a.a.

Struc: 66 a.a.

 Gene Ontology (GO) functional annotation 

• Biochemical function: DNA binding (2 terms)

DOI no: 10.1007/s10858-007-9204-4

J Biomol Nmr 40:1 (2008)

PubMed id: 18026911

High-resolution structure determination of the CylR2 homodimer using paramagnetic relaxation enhancement and structure-based prediction of molecular alignment.

S.Rumpel, S.Becker, M.Zweckstetter.

ABSTRACT

Structure determination of homooligomeric proteins by NMR spectroscopy is difficult due to the lack of chemical shift perturbation data, which is very effective in restricting the binding interface in heterooligomeric systems, and the difficulty of obtaining a sufficient number of intermonomer distance restraints. Here we solved the high-resolution solution structure of the 15.4 kDa homodimer CylR2, the regulator of cytolysin production from Enterococcus faecalis, which deviates by 1.1 A from the previously determined X-ray structure. We studied the influence of different experimental information such as long-range distances derived from paramagnetic relaxation enhancement, residual dipolar couplings, symmetry restraints and intermonomer Nuclear Overhauser Effect restraints on the accuracy of the derived structure. In addition, we show that it is useful to combine experimental information with methods of ab initio docking when the available experimental data are not sufficient to obtain convergence to the correct homodimeric structure. In particular, intermonomer distances may not be required when residual dipolar couplings are compared to values predicted on the basis of the charge distribution and the shape of ab initio docking solutions.