PDBsum entry 2rqw

Signaling protein

PDB id: 2rqw

Contents

Protein chains

105 a.a. *

24 a.a. *

* Residue conservation analysis

PDB id:

2rqw

Name:

Signaling protein

Title:

Solution structure of bem1p sh3ci domain complexed with ste20p-prr peptide

Structure:

Bud emergence protein 1. Chain: a. Fragment: sh3ci domain, residues 156-260. Synonym: bem1p, suppressor of rho3 protein 1. Engineered: yes. 24-meric peptide from serine/threonine-protein kinase ste20. Chain: b. Fragment: bem1-binding domain, residues 463-486.

Source:

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

NMR struc:

20 models

Authors:

T.Takaku,K.Ogura,F.Inagaki

Key ref:

T.Takaku et al. (2010). Solution structure of a novel Cdc42 binding module of Bem1 and its interaction with Ste20 and Cdc42. J Biol Chem, 285, 19346-19353. PubMed id: 20410294

Date:

21-Dec-09 Release date: 21-Apr-10

Protein chain

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

Seq: 551 a.a.

Struc: 105 a.a.

Protein chain

Q03497  (STE20_YEAST) -  Serine/threonine-protein kinase STE20 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: 939 a.a.

Struc: 24 a.a.

Enzyme reactions

• Enzyme class 1: Chain A: E.C.?
• Enzyme class 2: Chain B: E.C.2.7.11.1 - non-specific serine/threonine protein kinase.
• Reaction:
  1. L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H⁺
  2. L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + ADP + H⁺

Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

J Biol Chem 285:19346-19353 (2010)

PubMed id: 20410294

Solution structure of a novel Cdc42 binding module of Bem1 and its interaction with Ste20 and Cdc42.

T.Takaku, K.Ogura, H.Kumeta, N.Yoshida, F.Inagaki.

ABSTRACT

Bem1 is a scaffold protein essential for the establishment of cell polarity in Saccharomyces cerevisiae. This work reports the solution structure of a Cdc42 binding module of Bem1 comprising the second SH3 domain (SH3b) and its C-terminal flanking region termed Cdc42 interacting (CI). First, the structure of Bem1 SH3b-CI was determined by NMR spectroscopy, which shows that Bem1 SH3b-CI is a structurally and functionally related domain that binds Cdc42. Next, the solution structure of Bem1 SH3b-CI in complex with the proline-rich region of p21-activated kinase Ste20 (Ste20 PRR) was determined. Finally, the interaction surface of Bem1 SH3b-CI with Cdc42 was identified based on chemical shift perturbation studies which reveals that Bem1 SH3b-CI interacts simultaneously with both Ste20 PRR and Cdc42 using the opposite surfaces. Thus, Bem1 can tether Cdc42 and Ste20 in close proximity so that Cdc42 can efficiently interact with Ste20 Cdc42 and Rac interactive binding (CRIB). Based on the present results together with the previous biochemical studies (Lamson, R. E., Winters, M. J., and Pryciak, P. M. (2002) Mol. Cell. Biol. 22, 2939-2951 and Winters, M. J., and Pryciak, P. M. (2005) Mol. Cell. Biol. 25, 2177-2190), a model was suggested that the autoinhibition of Ste20 kinase activity by CRIB is released through the Cdc42-CRIB interaction, which is mediated by Bem1, and Ste20 is subsequently activated, an initial step for the establishment of the cell polarity.