PDBsum entry 1s7e

Transcription

PDB id: 1s7e

Contents

Protein chain

147 a.a. *

* Residue conservation analysis

PDB id:

1s7e

Name:

Transcription

Title:

Solution structure of hnf-6

Structure:

Hepatocyte nuclear factor 6. Chain: a. Fragment: DNA binging domain. Synonym: hnf-6, one cut domain family member 1. Engineered: yes

Source:

Mus musculus. House mouse. Organism_taxid: 10090. Strain: fvb-n. Organ: liver. Gene: rpod. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

NMR struc:

20 models

Authors:

X.Liao,W.Sheng

Key ref:

W.Sheng et al. (2004). Structure of the hepatocyte nuclear factor 6alpha and its interaction with DNA. J Biol Chem, 279, 33928-33936. PubMed id: 15169783 DOI: 10.1074/jbc.M403805200

Date:

29-Jan-04 Release date: 28-Dec-04

Protein chain

O08755  (HNF6_MOUSE) -  Hepatocyte nuclear factor 6 from Mus musculus

Seq: 465 a.a.

Struc: 147 a.a.

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1074/jbc.M403805200

J Biol Chem 279:33928-33936 (2004)

PubMed id: 15169783

Structure of the hepatocyte nuclear factor 6alpha and its interaction with DNA.

W.Sheng, H.Yan, F.M.Rausa, R.H.Costa, X.Liao.

ABSTRACT

Hepatocyte nuclear factor 6 (HNF-6) belongs to the family of One Cut transcription factors (also known as OC-1) and is essential for the development of the mouse pancreas, gall bladder, and the interhepatic bile ducts. HNF-6 binds to DNA as a monomer utilizing a single cut domain and a divergent homeodomain motif located at its C terminus. Here, we have used NMR methods to determine the solution structures of the 162 amino acid residue DNA-binding domain of the HNF-6alpha protein. The resulting overall structure of HNF-6alpha has two different distinct domains: the Cut domain and the Homeodomain connected by a long flexible linker. Our NMR structure shows that the Cut domain folds into a topology homologous to the POU DNA-binding domain, even though the sequences of these two protein families do not show homology. The DNA contact sequence of the HNF-6alpha was mapped with chemical shift perturbation methods. Our data also show that a proposed CREB-binding protein histone acetyltransferase protein-recruiting sequence, LSDLL, forms a helix and is involved in the hydrophobic core of the Cut domain. The structure implies that this sequence has to undergo structural changes when it interacts with CREB-binding protein.

Selected figure(s)

Figure 2.
FIG. 2. Separation structures of Cut domain and Homeodomain of HNF-6. A, best-fit superpositions of the 20 selected conformers with the lowest target functions from the final DYANA calculations colored as in Fig. 1. The Cut domain (red) and Homeodomain (blue) are separately superimposed on the regular secondary regions. B, ribbon backbone diagram of typical structures of the Cut domain (red) and Homeodomain (blue) with the lowest target functions.

Figure 4.
FIG. 4. The structural comparison of the Cut homeodomain of HNF-6 with the POU Homeodomain of Oct-1 (Protein Data Bank accession number 1e3o [PDB] ) (for review see Ref. 36). A, backbone stereotrace of the superposition of the Cut domain of HNF-6 with POU domain obtained from NMR structure. The Cut domain of HNF-6 is colored by red, and the POU domain is in green. B, the primary sequence and secondary structure alignment of the Cut domain and the POU domain. The conserved hydrophobic residues in the two domains are highlighted with yellow color. C, the Homeodomain of HNF-6 with homeodomain of Oct-1 obtained from x-ray crystal structure. Homeodomain of HNF-6 is colored by blue, and homeodomain of Oct-1 is in green. D, the primary sequence and secondary structure alignment of the two Homeodomains. The conserved hydrophobic residues in the two domains are highlighted with yellow color. Two unusual amino acid residues (Phe^147 and Met149) in the Homeodomain of HNF-6 are indicated with an asterisk.

The above figures are reprinted by permission from the ASBMB: J Biol Chem (2004, 279, 33928-33936) copyright 2004.

Figures were selected by an automated process.