PDBsum entry: 1ehx

Unknown function

PDB id: 1ehx

Contents

Protein chain

94 a.a. *

* Residue conservation analysis

PDB id:

1ehx

Name:

Unknown function

Title:

Nmr solution structure of the last unknown module of the cellulosomal scaffoldin protein cipc of clostridum cellulolyticum

Structure:

Scaffoldin protein. Chain: a. Fragment: unknow domain. Synonym: cipc. Other_details: homologous module with unknow function x2

Source:

Clostridium cellulolyticum. Organism_taxid: 1521

NMR struc:

20 models

Authors:

A.Mosbah,A.Belaich,O.Bornet,J.P.Belaich,B.Henrissat,H.Darbon

Key ref:

A.Mosbah et al. (2000). Solution structure of the module X2 1 of unknown function of the cellulosomal scaffolding protein CipC of Clostridium cellulolyticum. J Mol Biol, 304, 201-217. PubMed id: 11080456 DOI: 10.1006/jmbi.2000.4192

Date:

23-Feb-00 Release date: 17-Nov-00

Protein chain

Q45996  (Q45996_9CLOT) -  Scaffolding protein (Precursor)

Seq: 1546 a.a.

Struc: 94 a.a.*

* PDB and UniProt seqs differ at 3 residue positions (black crosses)

DOI no: 10.1006/jmbi.2000.4192

J Mol Biol 304:201-217 (2000)

PubMed id: 11080456

Solution structure of the module X2 1 of unknown function of the cellulosomal scaffolding protein CipC of Clostridium cellulolyticum.

A.Mosbah, A.Belaïch, O.Bornet, J.P.Belaïch, B.Henrissat, H.Darbon.

ABSTRACT

Multidimensional, homo- and heteronuclear magnetic resonance spectroscopy combined with dynamical annealing has been used to determine the structure of a 94 residue module (X2 1) of the scaffolding protein CipC from the anaerobic bacterium Clostridium cellulolyticum. An experimental data set comprising 1647 nuclear Overhauser effect-derived restraints, 105 hydrogen bond restraints and 66 phi torsion angle restraints was used to calculate 20 converging final solutions. The calculated structures have an average rmsd about the mean structure of 0.55(+/-0.11) A for backbone atoms and 1.40(+/-0.11) A for all heavy atoms when fitted over the secondary structural elements. The X2 1 module has an immunoglobulin-like fold with two beta-sheets packed against each other. One sheet contains three strands, the second contains four strands. An additional strand is intercalated between the beta-sandwich, as well as two turns of a 3(.10) helix. X2 1 has a surprising conformational stability and may act as a conformational linker and solubility enhancer within the scaffolding protein. The fold of X2 1 is very similar to that of telokin, titin Ig domain, hemolin D2 domain, twitchin immunoglobulin domain and the first four domains of the IgSF portion of transmembrane cell adhesion molecule. As a consequence, the X2 1 module is the first prokaryotic member assigned to the I set of the immunoglobulin superfamily even though no sequence similarity with any member of this superfamily could be detected.

Selected figure(s)

Figure 1.
Figure 1. Schematic representation of the modular organization of the scaffolding protein CipC of Clostridium cellulolyticum with eight cohesin modules (green), one cellulose binding module (yellow) and two X2 modules (red).

Figure 7.
Figure 7. Left: MOLSCRIPT ball and stick representation for the aromatic residues in the X2_1 module. Right: Superimposition of the hydrophobic core in the 20 structures of X2_1.

The above figures are reprinted by permission from Elsevier: J Mol Biol (2000, 304, 201-217) copyright 2000.

Figures were selected by an automated process.