PDBsum entry: 1zug

Transcription regulation

PDB id: 1zug

Contents

Protein chain

71 a.a. *

* Residue conservation analysis

PDB id:

1zug

Name:

Transcription regulation

Title:

Structure of phage 434 cro protein, nmr, 20 structures

Structure:

Phage 434 cro protein. Chain: a. Engineered: yes

Source:

Phage 434. Organism_taxid: 10712. Expressed in: escherichia coli. Expression_system_taxid: 562. Other_details: the plasmid was a gift from the laboratory of professor steve harrison (harvard university)

NMR struc:

20 models

Authors:

S.Padmanabhan,M.A.Jimenez,C.Gonzalez,J.M.Sanz,G.Gimenez- Gallego,M.Rico

Key ref:

S.Padmanabhan et al. (1997). Three-dimensional solution structure and stability of phage 434 Cro protein. Biochemistry, 36, 6424-6436. PubMed id: 9174359 DOI: 10.1021/bi970085p

Date:

14-Mar-97 Release date: 07-Jul-97

Protein chain

P03036  (RCRO_BP434) -  Regulatory protein cro

Seq: 71 a.a.

Struc: 71 a.a.

 Gene Ontology (GO) functional annotation 

• Biological process: regulation of transcription (3 terms)
• Biochemical function: DNA binding (3 terms)

DOI no: 10.1021/bi970085p

Biochemistry 36:6424-6436 (1997)

PubMed id: 9174359

Three-dimensional solution structure and stability of phage 434 Cro protein.

S.Padmanabhan, M.A.Jiménez, C.Gonzalez, J.M.Sanz, G.Giménez-Gallego, M.Rico.

ABSTRACT

1H NMR resonances of the phage 434 Cro protein were assigned using standard 2D NMR methods, and its solution structure determined using 867 distance constraints in distance geometry (DIANA) calculations ultimately refined by restrained molecular dynamics (GROMOS). In the 20 best NMR structures, the average pairwise backbone and heavy atom RMSDs are 0.63 +/- 0.14 and 1.53 +/- 0.15 A, respectively, for the structurally well-defined residues 4-65. Residues 1-3 and 66-71 at the N- and C-termini are structurally disordered. The region 4-65 includes five alpha-helices and tight turns which define the hydrophobic core of the protein. The backbone and heavy atom RMSDs for residues 4-65 are 0.92 +/- 0.12 and 1.99 +/- 0.12 A, respectively, for the NMR versus the crystal structures, but there are significant differences in the side-chain conformations and solvent accessibilities for some core residues. Analytical ultracentrifugation experiments confirm that 434 Cro is monomeric even at the high NMR concentrations. 434 Cro folding under NMR solution conditions is two-state as indicated by coincident urea denaturation curves from circular dichroism and intrinsic fluorescence measurements. They yield values for 434 Cro stability which show good correspondence to the free energy for global unfolding determined by NMR hydrogen exchange measurements for the slowest exchanging amide protons.