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5IP0

PHA Binding Protein PhaP (Phasin)

Summary for 5IP0
Entry DOI10.2210/pdb5ip0/pdb
DescriptorPHA granule-associated protein, CADMIUM ION (2 entities in total)
Functional Keywordsphb, polyhydroxyalkanoates, phap, biosurfactant, amphiphilicity, point mutation, emulsification, structural protein
Biological sourceAeromonas hydrophila
Total number of polymer chains16
Total formula weight205761.17
Authors
Chen, G.Q.,Wang, X.Q.,Zhao, H.Y. (deposition date: 2016-03-09, release date: 2017-01-25, Last modification date: 2024-03-20)
Primary citationZhao, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3 Å)
Structure validation

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