PDBsum entry 1qou

Plant protein

PDB id: 1qou

Contents

Protein chains

154 a.a. *

161 a.a. *

Waters ×283

* Residue conservation analysis

References listed in PDB file

Key reference

Title

The structure of antirrhinum centroradialis protein (cen) suggests a role as a kinase regulator.

Authors

M.J.Banfield, R.L.Brady.

Ref.

J Mol Biol, 2000, 297, 1159-1170. [DOI no: 10.1006/jmbi.2000.3619]

PubMed id

10764580

Abstract

Expression of the plant protein centroradialis (CEN) leads to a morphological switch between shoot growth and the development of flower structures (inflorescence). We have determined the crystal structure of Antirrhinum CEN to 1.9 A resolution. This structure confirms the CEN proteins as a subset of the family of phosphatidylethanolamine-binding proteins (PEBP), as predicted from sequence homology. Mammalian forms of PEBP have been found to act as inhibitors of MAP kinase signalling, a central signalling cascade regulating cell differentiation. CEN and PEBP proteins share a similar topology dominated by a large central beta-sheet. The strong conservation of a binding pocket at one end of this sheet which is capable of binding phosphoryl ligands, suggests the biological effects of CEN, like PEBP, arise from the ability of this region to form complexes with phosphorylated ligands, hence interfering with kinases and their effectors.

Figure 2.
Figure 2. (a) MOLSCRIPT [Kraulis 1991] representation of the crystal structure of Antirrhinum CEN. The invariant histidine (His86) in the ligand-binding site is shown in yellow in ball-and-stick representation. The Figure was prepared with BOBSCRIPT [Esnouf 1997], and rendered with Raster3D [Merritt and Bacon 1997]. (b) Stereoview showing the C^a traces of the crystal structure of Antirrhinum CEN superimposed on the structure of human PEBP. CEN (green) and hPEBP (red lines). The amino and carboxy termini are labelled N and C, respectively, and the side-chain for His86 is shown yellow. The Figure was prepared with BOBSCRIPT [Esnouf 1997].

Figure 5.
Figure 5. The arrangement of conserved residues forming the ligand-binding site in (a) bPEBP, (b) hPEBP and (c) CEN. Each model is in approximately the same orientation. The location of the bound phosphoryl group (PE) is shown with bPEBP [Serre et al 1998] in (a), and the location of the bound cacodylate ion (labelled CAC) is shown with hPEBP in (b). Hydrogen bonds are shown as broken magenta lines.

The above figures are reprinted by permission from Elsevier: J Mol Biol (2000, 297, 1159-1170) copyright 2000.

Secondary reference #1

Title

Function from structure? the crystal structure of human phosphatidylethanolamine-Binding protein suggests a role in membrane signal transduction.

Authors

M.J.Banfield, J.J.Barker, A.C.Perry, R.L.Brady.

Ref.

Structure, 1998, 6, 1245-1254. [DOI no: 10.1016/S0969-2126(98)00125-7]

PubMed id

9782050

Figure 3.
Figure 3. Secondary structure elements in hPEBP. (a) The putative dimer of hPEBP formed by the two molecules in the asymmetric unit of the crystal. Also shown (arrow) is the approximate direction of the dipole moment for the hPEBP dimer, which suggests an orientation for the oligomer to interact with the membrane. The molecules of cacodylate present in the ligand-bound structure are shown in CPK representation. (b) Schematic topology diagram illustrating the arrangement of secondary structure in the hPEBP monomer. β Strands (shown in cyan) are labelled with lower-case letters and correspond to immunoglobulin/fibronectin type III conventions, as discussed in the text; α helices (shown in red) are labelled with upper-case letters. (The figures were prepared using the program MOLSCRIPT [32] and rendered using Raster3D [33].)

The above figure is reproduced from the cited reference with permission from Cell Press

Secondary reference #2

Title

Crystal structure of the phosphatidylethanolamine-Binding protein from bovine brain: a novel structural class of phospholipid-Binding proteins.

Authors

L.Serre, B.Vallée, N.Bureaud, F.Schoentgen, C.Zelwer.

Ref.

Structure, 1998, 6, 1255-1265. [DOI no: 10.1016/S0969-2126(98)00126-9]

PubMed id

9782057

Figure 3.
Figure 3. The electrostatic surface potential of PEBP. The bound phosphorylethanolamine is shown in the cavity in ball-and-stick representation. Regions of negative potential are shown in red; regions of positive potential are in blue. The strip of basic residues is labeled in yellow. CR1 and CR2 represent strand-connecting regions 1 and 2, respectively. (The figure was created using the program GRASP [25].)

The above figure is reproduced from the cited reference with permission from Cell Press