1EHX

NMR SOLUTION STRUCTURE OF THE LAST UNKNOWN MODULE OF THE CELLULOSOMAL SCAFFOLDIN PROTEIN CIPC OF CLOSTRIDUM CELLULOLYTICUM

1EHX の概要

• エントリーDOI: 10.2210/pdb1ehx/pdb
• NMR情報: BMRB: 4589
• 分子名称: SCAFFOLDIN PROTEIN (1 entity in total)
• 機能のキーワード: beta-beta-barrels, 3.10 helix, unknown function
• 由来する生物種: Clostridium cellulolyticum
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 10042.23

構造登録者

Mosbah, A.,Belaich, A.,Bornet, O.,Belaich, J.P.,Henrissat, B.,Darbon, H. (登録日: 2000-02-23, 公開日: 2000-11-17, 最終更新日: 2024-05-22)

主引用文献

Mosbah, A.,Belaich, A.,Bornet, O.,Belaich, J.P.,Henrissat, B.,Darbon, H.
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, 2000

PubMed 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.

PubMed: 11080456
DOI: 10.1006/jmbi.2000.4192

実験手法

SOLUTION NMR