PDBsum entry 2kfk

Signaling protein

PDB id: 2kfk

Contents

Protein chains

78 a.a. *

86 a.a. *

* Residue conservation analysis

PDB id:

2kfk

Name:

Signaling protein

Title:

Solution structure of bem1p pb1 domain complexed with cdc24p pb1 domain

Structure:

Bud emergence protein 1. Chain: a. Fragment: unp residues 477-551. Synonym: suppressor of rho3 protein 1. Engineered: yes. Cell division control protein 24. Chain: b. Fragment: unp residues 761-854. Synonym: calcium regulatory protein.

Source:

Saccharomyces cerevisiae. Yeast. Organism_taxid: 4932. Expressed in: escherichia coli. Expression_system_taxid: 562.

NMR struc:

20 models

Authors:

Y.Kobashigawa,S.Yoshinaga,T.Tandai,K.Ogura,F.Inagaki

Key ref:

K.Ogura et al. (2009). NMR structure of the heterodimer of Bem1 and Cdc24 PB1 domains from Saccharomyces cerevisiae. J Biochem (tokyo), 146, 317-325. PubMed id: 19451149

Date:

23-Feb-09 Release date: 06-Oct-09

Protein chain

P29366  (BEM1_YEAST) -  Bud emergence protein 1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: 551 a.a.

Struc: 78 a.a.*

Protein chain

P11433  (CDC24_YEAST) -  Cell division control protein 24 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: 854 a.a.

Struc: 86 a.a.*

* PDB and UniProt seqs differ at 5 residue positions (black crosses)

J Biochem (tokyo) 146:317-325 (2009)

PubMed id: 19451149

NMR structure of the heterodimer of Bem1 and Cdc24 PB1 domains from Saccharomyces cerevisiae.

K.Ogura, T.Tandai, S.Yoshinaga, Y.Kobashigawa, H.Kumeta, T.Ito, H.Sumimoto, F.Inagaki.

ABSTRACT

Bem1 and Cdc24 of the budding yeast Saccharomyces cerevisiae interact with each other through PB1-PB1 heterodimer formation to regulate the establishment of cell polarity. Here we present the tertiary structure of the heterodimer of Bem1 and Cdc24 PB1 domains determined by NMR spectroscopy. To avoid ambiguity in the NMR spectral analysis, we first prepared a mutant of the Cdc24 PB1 domain that had truncated loops. The mutant provided well dispersed spectra without spectral overlapping, thus allowing unambiguous spectral assignments for structure determination. We confirmed that the loop deletion-mutant was quite similar to the wild-type in both 3D structure and binding affinity. The NMR structure of the heterodimer of the deletion-mutant of Cdc24 PB1 and Bem1 PB1 was determined using a variety of isotope labelled samples including perdeuteration. The interface between the Bem1/Cdc24 PB1 heterodimer was analysed at atomic resolution. Through a comparison with the tertiary structures of other PB1-PB1 heterodimers, we found that conserved electrostatic properties on the molecular surface were commonly used for PB1-PB1 interaction, but hydrophobic interactions were important for cognate interaction in Bem1/Cdc24 PB1 heterodimer formation.