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| | <StructureSection load='5ip0' size='340' side='right'caption='[[5ip0]], [[Resolution|resolution]] 3.00Å' scene=''> | | <StructureSection load='5ip0' size='340' side='right'caption='[[5ip0]], [[Resolution|resolution]] 3.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5ip0]] is a 16 chain structure with sequence from [http://en.wikipedia.org/wiki/"aeromonas_liquefaciens"_kluyver_and_van_niel_1936 "aeromonas liquefaciens" kluyver and van niel 1936]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5IP0 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5IP0 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5ip0]] is a 16 chain structure with sequence from [https://en.wikipedia.org/wiki/Aeromonas_hydrophila Aeromonas hydrophila]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5IP0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5IP0 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">phaP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=644 "Aeromonas liquefaciens" Kluyver and van Niel 1936])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5ip0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ip0 OCA], [http://pdbe.org/5ip0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ip0 RCSB], [http://www.ebi.ac.uk/pdbsum/5ip0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ip0 ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5ip0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ip0 OCA], [https://pdbe.org/5ip0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ip0 RCSB], [https://www.ebi.ac.uk/pdbsum/5ip0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ip0 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/O32470_AERHY O32470_AERHY] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Aeromonas liquefaciens kluyver and van niel 1936]] | + | [[Category: Aeromonas hydrophila]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Chen, G Q]] | + | [[Category: Chen GQ]] |
| - | [[Category: Wang, X Q]] | + | [[Category: Wang XQ]] |
| - | [[Category: Zhao, H Y]] | + | [[Category: Zhao HY]] |
| - | [[Category: Amphiphilicity]]
| + | |
| - | [[Category: Biosurfactant]]
| + | |
| - | [[Category: Emulsification]]
| + | |
| - | [[Category: Phap]]
| + | |
| - | [[Category: Phb]]
| + | |
| - | [[Category: Point mutation]]
| + | |
| - | [[Category: Polyhydroxyalkanoate]]
| + | |
| - | [[Category: Structural protein]]
| + | |
| Structural highlights
Function
O32470_AERHY
Publication Abstract from PubMed
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 (PhaPAh), which is utilized in protein and tissue engineering. The crystal structure of PhaPAh was revealed to be a tetramer with 8 alpha-helices adopting a coiled-coil structure. Each monomer has a hydrophobic and a hydrophilic surface, rendering the surfactant properties of the PhaPAh 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.
Structural Insights on PHA Binding Protein PhaP from Aeromonas hydrophila.,Zhao H, Wei H, Liu X, Yao Z, Xu M, Wei D, Wang J, Wang X, Chen GQ Sci Rep. 2016 Dec 23;6:39424. doi: 10.1038/srep39424. PMID:28009010[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Zhao H, Wei H, Liu X, Yao Z, Xu M, Wei D, Wang J, Wang X, Chen GQ. Structural Insights on PHA Binding Protein PhaP from Aeromonas hydrophila. Sci Rep. 2016 Dec 23;6:39424. doi: 10.1038/srep39424. PMID:28009010 doi:http://dx.doi.org/10.1038/srep39424
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