2gvm: Difference between revisions
New page: left|200px<br /><applet load="2gvm" size="450" color="white" frame="true" align="right" spinBox="true" caption="2gvm, resolution 2.300Å" /> '''Crystal structure o... |
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[[Image:2gvm.gif|left|200px]]<br /><applet load="2gvm" size=" | [[Image:2gvm.gif|left|200px]]<br /><applet load="2gvm" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="2gvm, resolution 2.300Å" /> | caption="2gvm, resolution 2.300Å" /> | ||
'''Crystal structure of hydrophobin HFBI with detergent'''<br /> | '''Crystal structure of hydrophobin HFBI with detergent'''<br /> | ||
==Overview== | ==Overview== | ||
Hydrophobins are small fungal proteins that are highly surface active and | Hydrophobins are small fungal proteins that are highly surface active and possess a unique ability to form amphiphilic membranes through spontaneous self-assembly. The first crystal structure of a hydrophobin, Trichoderma reesei HFBII, revealed the structural basis for the function of this amphiphilic protein--a patch consisting of hydrophobic side chains on the protein surface. Here, the crystal structures of a native and a variant T. reesei hydrophobin HFBI are presented, revealing the same overall structure and functional hydrophobic patch as in the HFBII structure. However, some structural flexibility was found in the native HFBI structure: The asymmetric unit contained four molecules, and, in two of these, an area of seven residues was displaced as compared to the two other HFBI molecules and the previously determined HFBII structure. This structural change is most probably induced by multimer formation. Both the native and the N-Cys-variant of HFBI were crystallized in the presence of detergents, but an association between the protein and a detergent was only detected in the variant structure. There, the molecules were arranged into an extraordinary detergent-associated octamer and the solvent content of the crystals was 75%. This study highlights the conservation of the fold of class II hydrophobins in spite of the low sequence identity and supports our previous suggestion that concealment of the hydrophobic surface areas of the protein is the driving force in the formation of multimers and monolayers in the self-assembly process. | ||
==About this Structure== | ==About this Structure== | ||
2GVM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Hypocrea_jecorina Hypocrea jecorina] with ZN and LDA as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | 2GVM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Hypocrea_jecorina Hypocrea jecorina] with <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=LDA:'>LDA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GVM OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Hypocrea jecorina]] | [[Category: Hypocrea jecorina]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Hakanpaa, J | [[Category: Hakanpaa, J M.]] | ||
[[Category: Rouvinen, J.]] | [[Category: Rouvinen, J.]] | ||
[[Category: LDA]] | [[Category: LDA]] | ||
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[[Category: surfactant]] | [[Category: surfactant]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:35:51 2008'' | ||
Revision as of 18:35, 21 February 2008
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Crystal structure of hydrophobin HFBI with detergent
OverviewOverview
Hydrophobins are small fungal proteins that are highly surface active and possess a unique ability to form amphiphilic membranes through spontaneous self-assembly. The first crystal structure of a hydrophobin, Trichoderma reesei HFBII, revealed the structural basis for the function of this amphiphilic protein--a patch consisting of hydrophobic side chains on the protein surface. Here, the crystal structures of a native and a variant T. reesei hydrophobin HFBI are presented, revealing the same overall structure and functional hydrophobic patch as in the HFBII structure. However, some structural flexibility was found in the native HFBI structure: The asymmetric unit contained four molecules, and, in two of these, an area of seven residues was displaced as compared to the two other HFBI molecules and the previously determined HFBII structure. This structural change is most probably induced by multimer formation. Both the native and the N-Cys-variant of HFBI were crystallized in the presence of detergents, but an association between the protein and a detergent was only detected in the variant structure. There, the molecules were arranged into an extraordinary detergent-associated octamer and the solvent content of the crystals was 75%. This study highlights the conservation of the fold of class II hydrophobins in spite of the low sequence identity and supports our previous suggestion that concealment of the hydrophobic surface areas of the protein is the driving force in the formation of multimers and monolayers in the self-assembly process.
About this StructureAbout this Structure
2GVM is a Single protein structure of sequence from Hypocrea jecorina with and as ligands. Full crystallographic information is available from OCA.
ReferenceReference
Two crystal structures of Trichoderma reesei hydrophobin HFBI--the structure of a protein amphiphile with and without detergent interaction., Hakanpaa J, Szilvay GR, Kaljunen H, Maksimainen M, Linder M, Rouvinen J, Protein Sci. 2006 Sep;15(9):2129-40. Epub 2006 Aug 1. PMID:16882996
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