4P99

Ca2+-stabilized adhesin helps an Antarctic bacterium reach out and bind ice

4P99 の概要

• エントリーDOI: 10.2210/pdb4p99/pdb
• 分子名称: MpAFP_RII tetra-tandemer, CALCIUM ION, 1,2-ETHANEDIOL, ... (6 entities in total)
• 機能のキーワード: ca2+-dependent, bacterial ig-like fold, ice-binding adhesin, extender domain, unknown function
• 由来する生物種: Marinomonas primoryensis
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 178378.45

構造登録者

Guo, S.,Vance, D.R.T.,Campbell, R.L.,Davies, P.L. (登録日: 2014-04-02, 公開日: 2014-06-18, 最終更新日: 2023-12-27)

主引用文献

Vance, T.D.,Olijve, L.L.,Campbell, R.L.,Voets, I.K.,Davies, P.L.,Guo, S.
Ca2+-stabilized adhesin helps an Antarctic bacterium reach out and bind ice.
Biosci.Rep., 34:-, 2014

PubMed Abstract: The large size of a 1.5-MDa ice-binding adhesin [MpAFP (Marinomonas primoryensis antifreeze protein)] from an Antarctic Gram-negative bacterium, M. primoryensis, is mainly due to its highly repetitive RII (Region II). MpAFP_RII contains roughly 120 tandem copies of an identical 104-residue repeat. We have previously determined that a single RII repeat folds as a Ca2+-dependent immunoglobulin-like domain. Here, we solved the crystal structure of RII tetra-tandemer (four tandem RII repeats) to a resolution of 1.8 Å. The RII tetra-tandemer reveals an extended (~190-Å × ~25-Å), rod-like structure with four RII-repeats aligned in series with each other. The inter-repeat regions of the RII tetra-tandemer are strengthened by Ca2+ bound to acidic residues. SAXS (small-angle X-ray scattering) profiles indicate the RII tetra-tandemer is significantly rigidified upon Ca2+ binding, and that the protein's solution structure is in excellent agreement with its crystal structure. We hypothesize that >600 Ca2+ help rigidify the chain of ~120 104-residue repeats to form a ~0.6 μm rod-like structure in order to project the ice-binding domain of MpAFP away from the bacterial cell surface. The proposed extender role of RII can help the strictly aerobic, motile bacterium bind ice in the upper reaches of the Antarctic lake where oxygen and nutrients are most abundant. Ca2+-induced rigidity of tandem Ig-like repeats in large adhesins might be a general mechanism used by bacteria to bind to their substrates and help colonize specific niches.

PubMed: 24892750
DOI: 10.1042/BSR20140083

実験手法

X-RAY DIFFRACTION (1.8 Å)