PDBsum entry 1f43

Transcription

PDB id: 1f43

Contents

Protein chain

61 a.a. *

* Residue conservation analysis

PDB id:

1f43

Name:

Transcription

Title:

Solution structure of the mata1 homeodomain

Structure:

Mating-type protein a-1. Chain: a. Fragment: homeodomain, c-terminal domain (66-126). Engineered: yes

Source:

Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932. Expressed in: escherichia coli. Expression_system_taxid: 562.

NMR struc:

20 models

Authors:

J.S.Anderson,M.Forman,S.Modleski,F.W.Dahlquist,S.M.Baxter

Key ref:

J.S.Anderson et al. (2000). Cooperative ordering in homeodomain-DNA recognition: solution structure and dynamics of the MATa1 homeodomain. Biochemistry, 39, 10045-10054. PubMed id: 10955992 DOI: 10.1021/bi000677z

Date:

07-Jun-00 Release date: 26-Jul-00

Protein chain

P0CY10  (MATA1_YEASX) -  Mating-type protein A1 from Saccharomyces cerevisiae

Seq: 126 a.a.

Struc: 61 a.a.

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1021/bi000677z

Biochemistry 39:10045-10054 (2000)

PubMed id: 10955992

Cooperative ordering in homeodomain-DNA recognition: solution structure and dynamics of the MATa1 homeodomain.

J.S.Anderson, M.D.Forman, S.Modleski, F.W.Dahlquist, S.M.Baxter.

ABSTRACT

The mating type homeodomain proteins, MATa1 and MATalpha2, combine to form a heterodimer to bind DNA in diploid yeast cells. The a1-alpha2 heterodimer tightly and specifically binds haploid-specific gene operators to repress transcription. On its own, however, the a1 homeodomain does not bind DNA in a sequence-specific manner. To help understand this interaction, we describe the solution structure and backbone dynamics of the free a1 homeodomain. Free a1 in solution is an ensemble of structures having flexible hinges at the two turns in the small protein fold. Conformational changes in the a1 homeodomain upon ternary complex formation are located in the loop between helix 1 and helix 2, where the C-terminal tail of alpha2 binds to form the heterodimer, and at the C-terminus of helix 3, the DNA recognition helix. The observed differences, comparing the free and bound a1 structures, suggest a mechanism linking van der Waals stacking changes to the ordering of a final turn in the DNA-binding helix of a1. The tail of alpha2 induces changes in loop 1 of a1 that push it toward a properly folded DNA binding conformation.