5IP0

PHA Binding Protein PhaP (Phasin)

5IP0 の概要

• エントリーDOI: 10.2210/pdb5ip0/pdb
• 分子名称: PHA granule-associated protein, CADMIUM ION (2 entities in total)
• 機能のキーワード: phb, polyhydroxyalkanoates, phap, biosurfactant, amphiphilicity, point mutation, emulsification, structural protein
• 由来する生物種: Aeromonas hydrophila
• タンパク質・核酸の鎖数: 16
• 化学式量合計: 205761.17

構造登録者

Chen, G.Q.,Wang, X.Q.,Zhao, H.Y. (登録日: 2016-03-09, 公開日: 2017-01-25, 最終更新日: 2024-03-20)

主引用文献

Zhao, H.,Wei, H.,Liu, X.,Yao, Z.,Xu, M.,Wei, D.,Wang, J.,Wang, X.,Chen, G.Q.
Structural Insights on PHA Binding Protein PhaP from Aeromonas hydrophila
Sci Rep, 6:39424-39424, 2016

PubMed Abstract: Phasins or PhaPs are a group of amphiphilic proteins that are found attached to the surface of microbial polyhydroxyalkanoate (PHA) granules. They have both structural and regulatory functions and can affect intracellular PHA accumulation and mediate protein folding. The molecular basis for the diverse functions of the PhaPs has not been fully understood due to the lack of the structural knowledge. Here we report the structural and biochemical studies of the PhaP cloned from Aeromonas hydrophila (PhaP), which is utilized in protein and tissue engineering. The crystal structure of PhaP was revealed to be a tetramer with 8 α-helices adopting a coiled-coil structure. Each monomer has a hydrophobic and a hydrophilic surface, rendering the surfactant properties of the PhaP monomer. Based on the crystal structure, we predicted three key amino acid residues and obtained mutants with enhanced stability and improved emulsification properties. The first PhaP crystal structure, as reported in this study, is an important step towards a mechanistic understanding of how PHA is formed in vivo and why PhaP has such unique surfactant properties. At the same time, it will facilitate the study of other PhaP members that may have significant biotechnological potential as bio-surfactants and amphipathic coatings.

PubMed: 28009010
DOI: 10.1038/srep39424

実験手法

X-RAY DIFFRACTION (3 Å)