3ENT

Crystal structure of Nitrollin, a betagamma-crystallin from Nitrosospira multiformis-in alternate space group (P65)

3ENT の概要

• エントリーDOI: 10.2210/pdb3ent/pdb
• 関連するPDBエントリー: 3enu
• 分子名称: Putative uncharacterized protein (2 entities in total)
• 機能のキーワード: betagamma crystallin, structural protein
• 由来する生物種: Nitrosospira multiformis
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 26650.35

構造登録者

Aravind, P.,Sankaranarayanan, R. (登録日: 2008-09-26, 公開日: 2009-03-31, 最終更新日: 2024-10-16)

主引用文献

Aravind, P.,Suman, S.K.,Mishra, A.,Sharma, Y.,Sankaranarayanan, R.
Three-dimensional domain swapping in nitrollin, a single-domain betagamma-crystallin from Nitrosospira multiformis, controls protein conformation and stability but not dimerization
J.Mol.Biol., 385:163-177, 2009

PubMed Abstract: The betagamma-crystallin superfamily has a well-characterized protein fold, with several members found in both prokaryotic and eukaryotic worlds. A majority of them contain two betagamma-crystallin domains. A few examples, such as ciona crystallin and spherulin 3a exist that represent the eukaryotic single-domain proteins of this superfamily. This study reports the high-resolution crystal structure of a single-domain betagamma-crystallin protein, nitrollin, from the ammonium-oxidizing soil bacterium Nitrosospira multiformis. The structure retains the characteristic betagamma-crystallin fold despite a very low sequence identity. The protein exhibits a unique case of homodimerization in betagamma-crystallins by employing its N-terminal extension to undergo three-dimensional (3D) domain swapping with its partner. Removal of the swapped strand results in partial loss of structure and stability but not dimerization per se as determined using gel filtration and equilibrium unfolding studies. Overall, nitrollin represents a distinct single-domain prokaryotic member that has evolved a specialized mode of dimerization hitherto unknown in the realm of betagamma-crystallins.

PubMed: 18976659
DOI: 10.1016/j.jmb.2008.10.035

実験手法

X-RAY DIFFRACTION (2.14 Å)