PDBsum entry 1k1c

Transport protein

PDB id: 1k1c

Contents

Protein chain

84 a.a. *

* Residue conservation analysis

PDB id:

1k1c

Name:

Transport protein

Title:

Solution structure of crh, the bacillus subtilis catabolite repression hpr

Structure:

Catabolite repression hpr-like protein. Chain: a. Engineered: yes

Source:

Bacillus subtilis. Organism_taxid: 1423. Expressed in: escherichia coli. Expression_system_taxid: 562

NMR struc:

24 models

Authors:

A.Favier,B.Brutscher,M.Blackledge,A.Galinier,J.Deutscher,F.Penin, D.Marion

Key ref:

A.Favier et al. (2002). Solution structure and dynamics of Crh, the Bacillus subtilis catabolite repression HPr. J Mol Biol, 317, 131-144. PubMed id: 11916384 DOI: 10.1006/jmbi.2002.5397

Date:

25-Sep-01 Release date: 17-Oct-01

Protein chain

O06976  (CRH_BACSU) -  HPr-like protein Crh from Bacillus subtilis (strain 168)

Seq: 85 a.a.

Struc: 84 a.a.

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1006/jmbi.2002.5397

J Mol Biol 317:131-144 (2002)

PubMed id: 11916384

Solution structure and dynamics of Crh, the Bacillus subtilis catabolite repression HPr.

A.Favier, B.Brutscher, M.Blackledge, A.Galinier, J.Deutscher, F.Penin, D.Marion.

ABSTRACT

The solution structure and dynamics of the Bacillus subtilis HPr-like protein, Crh, have been investigated using NMR spectroscopy. Crh exhibits high sequence identity (45 %) to the histidine-containing protein (HPr), a phospho-carrier protein of the phosphoenolpyruvate (PEP):carbohydrate phosphotransferase system, but contains no catalytic His15, the site of PEP-dependent phosphorylation in HPr. Crh also forms a mixture of monomers and dimers in solution whereas HPr is known to be monomeric. Complete backbone and side-chain assignments were obtained for the monomeric form, and 60 % of the dimer backbone resonances; allowing the identification of the Crh dimer interface from chemical-shift mapping. The conformation of Crh was determined to a precision of 0.46(+/-0.06) A for the backbone atoms, and 1.01(+/-0.08) A for the heavy atoms. The monomer structure is similar to that of known HPr 2.67(+/-0.22) A (C(alpha) rmsd), but has a few notable differences, including a change in the orientation of one of the helices (B), and a two-residue shift in beta-sheet pairing of the N-terminal strand with the beta4 strand. This shift results in a shortening of the surface loop present in HPr and consequently provides a flatter surface in the region of dimerisation contact, which may be related to the different oligomeric nature of these two proteins. A binding site of phospho-serine(P-Ser)-Crh with catabolite control protein A (CcpA) is proposed on the basis of highly conserved surface side-chains between Crh and HPr. This binding site is consistent with the model of a dimer-dimer interaction between P-Ser-Crh and CcpA. (15)N relaxation measured in the monomeric form also identified differential local mobility in the helix B which is located in the vicinity of this site.

Selected figure(s)

Figure 7.
Figure 7. Comparison of binding surface for enzyme I and enzyme IIA^Glc on E. coliHPr to the corresponding surface ofB. subtilis HPr and Crh. The PDB entries used forE. coliHPr, B. subtilis HPr and Crh are 1HDN,[31] 2HID [40] and 1K1C, respectively. (a) The residues of helices A and B, involved in analogous hydrophobic and/or electrostatic interactions in the (HPr-EIN)E. coli and (HPr-enzyme IIA^Glc)E. coli complexes and conserved inB. subtilis HPr are highlighted on the HPr surfaces. The residues, whose side-chains participate in hydrophobic and electrostatic interactions, are colored in green and blue, respectively. The PTS active site residue His15 is indicated in red and the CCR regulation site residue Ser46 in B. subtilis is indicated in yellow. The corresponding residues of B. subtilis Crh are colored in the same way but Gln15 of Crh is colored in magenta. Leu50 of Crh, which is part of the central hydrophobic core, is colored in dark green. (b) Stick representation of the residues colored in (a). (c) Same picture as in (a) but containing also residues situated around the hydrophobic core involved in hydrophobic and/or electrostatic interactions in the (HPr-EIN)E. coli and (HPr-enzyme IIA^Glc)E. coli complexes, but which are only partly conserved in B. subtilis HPr and Crh.

Figure 9.
Figure 9. Diagram showing the two proposed models for Crh dimer topology. (a) direct association via the L1 and L2 loops. (b) Association via the swapping of the b1 strand.

The above figures are reprinted by permission from Elsevier: J Mol Biol (2002, 317, 131-144) copyright 2002.

Figures were selected by an automated process.