PDBsum entry 1fux

Unknown function

PDB id: 1fux

Contents

Protein chains

165 a.a. *

Waters ×206

* Residue conservation analysis

PDB id:

1fux

Name:

Unknown function

Title:

Crystal structure of e.Coli ybcl, a new member of the mammalian pebp family

Structure:

Hypothetical 19.5 kda protein in emre-rus intergenic region. Chain: a, b. Engineered: yes. Other_details: periplasmic form

Source:

Escherichia coli. Organism_taxid: 562. Expressed in: escherichia coli. Expression_system_taxid: 562.

Biol. unit:

Dimer (from PQS)

Resolution:

1.81Å R-factor: 0.200 R-free: 0.254

Authors:

L.Serre,K.Pereira De Jesus,H.Benedetti,N.Bureaud,F.Schoentgen, C.Zelwer

Key ref:

L.Serre et al. (2001). Crystal structures of YBHB and YBCL from Escherichia coli, two bacterial homologues to a Raf kinase inhibitor protein. J Mol Biol, 310, 617-634. PubMed id: 11439028 DOI: 10.1006/jmbi.2001.4784

Date:

18-Sep-00 Release date: 18-Jul-01

Protein chains

P77368  (YBCL_ECOLI) -  UPF0098 protein YbcL from Escherichia coli (strain K12)

Seq: 183 a.a.

Struc: 165 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

DOI no: 10.1006/jmbi.2001.4784

J Mol Biol 310:617-634 (2001)

PubMed id: 11439028

Crystal structures of YBHB and YBCL from Escherichia coli, two bacterial homologues to a Raf kinase inhibitor protein.

L.Serre, K.Pereira de Jesus, C.Zelwer, N.Bureaud, F.Schoentgen, H.Bénédetti.

ABSTRACT

In rat and human cells, RKIP (previously known as PEBP) was characterized as an inhibitor of the MEK phosphorylation by Raf-1. In Escherichia coli, the genes ybhb and ybcl possibly encode two RKIP homologues while in the genomes of other bacteria and archaebacteria other homologous genes of RKIP have been found. The parallel between the cellular signaling mechanisms in eukaryotes and prokaryotes suggests that these bacterial proteins could be involved in the regulation of protein phosphorylation by kinases as well. We first showed that the proteins YBHB and YBCL were present in the cytoplasm and periplasm of E. coli, respectively, after which we determined their crystallographic structures. These structures verify that YBHB and YBCL belong to the same structural family as mammalian RKIP/PEBP proteins. The general fold and the anion binding site of these proteins are extremely well conserved between mammals and bacteria and suggest functional similarities. However, the bacterial proteins also exhibit some specific structural features, like a substrate binding pocket formed by the dimerization interface and the absence of cis peptide bonds. This structural variety should correspond to the recognition of multiple cellular partners.

Selected figure(s)

Figure 6.
Figure 6. Superposition of the binding sites of YBHB and YBCL. Only residues with distinct confor- mations have been represented by ball-and-sticks. Magenta for YBHB residues and green for YBCL resi- dues. C a atoms of YBHB are painted in pale pink and C a atoms of YBCL in pale green (Figure generated by RIBBONS).

Figure 10.
Figure 10. Binding sites of YBHB, YBCL, PEBP complexed with phosphoryl-ethanolamine and CEN. The structures are rep- resented with the same orientation. H-bonds are schematized by bro- ken lines. Only conserved or water molecules discussed are drawn. (a) YBHB, (b) YBCL, (c) PEBP, (d) CEN (Figures generated by MOLSCRIPT and Raster3D).

The above figures are reprinted by permission from Elsevier: J Mol Biol (2001, 310, 617-634) copyright 2001.

Figures were selected by an automated process.