2pl7
From Proteopedia
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==Overview== | ==Overview== | ||
| - | Hydrophobins are small, amphiphilic proteins secreted by filamentous | + | Hydrophobins are small, amphiphilic proteins secreted by filamentous fungi. Their functionality arises from a patch of hydrophobic residues on the protein surface. Spontaneous self-assembly of hydrophobins leads to the formation of an amphiphilic layer that remarkably reduces the surface tension of water. We have determined by x-ray diffraction two new crystal structures of Trichoderma reesei hydrophobin HFBII in the presence of a detergent. The monoclinic crystal structure (2.2A resolution, R = 22, R(free) = 28) is composed of layers of hydrophobin molecules where the hydrophobic surface areas of the molecules are aligned within the layer. Viewed perpendicular to the aligned hydrophobic surface areas, the molecules in the layer pack together to form six-membered rings, thus leaving small pores in the layer. Similar packing has been observed in the atomic force microscopy images of the self-assembled layers of class II hydrophobin, indicating that the crystal structure resembles that of natural hydrophobin film. The orthorhombic crystal structure (1.0 A resolution, R = 13, R(free) = 15) is composed of fiber-like arrays of protein molecules. Rodlet structures have been observed on amphiphilic layers formed by class I hydrophobins; fibrils of class II hydrophobins appear by vigorous shaking. We propose that the structure of the fibrils and/or rodlets is similar to that observed in the crystal structure. |
==About this Structure== | ==About this Structure== | ||
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==Reference== | ==Reference== | ||
| - | Crystal | + | Crystal structures of hydrophobin HFBII in the presence of detergent implicate the formation of fibrils and monolayer films., Kallio JM, Linder MB, Rouvinen J, J Biol Chem. 2007 Sep 28;282(39):28733-9. Epub 2007 Jul 18. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17636262 17636262] |
[[Category: Hypocrea jecorina]] | [[Category: Hypocrea jecorina]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Kallio, J | + | [[Category: Kallio, J M.]] |
| - | [[Category: Rouvinen, J | + | [[Category: Rouvinen, J P.]] |
[[Category: HTG]] | [[Category: HTG]] | ||
[[Category: SO4]] | [[Category: SO4]] | ||
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[[Category: surface active protein]] | [[Category: surface active protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:30:37 2008'' |
Revision as of 16:30, 21 February 2008
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Orhorhombic crystal structure of hydrophobin HFBII in the presence of a detergent
Overview
Hydrophobins are small, amphiphilic proteins secreted by filamentous fungi. Their functionality arises from a patch of hydrophobic residues on the protein surface. Spontaneous self-assembly of hydrophobins leads to the formation of an amphiphilic layer that remarkably reduces the surface tension of water. We have determined by x-ray diffraction two new crystal structures of Trichoderma reesei hydrophobin HFBII in the presence of a detergent. The monoclinic crystal structure (2.2A resolution, R = 22, R(free) = 28) is composed of layers of hydrophobin molecules where the hydrophobic surface areas of the molecules are aligned within the layer. Viewed perpendicular to the aligned hydrophobic surface areas, the molecules in the layer pack together to form six-membered rings, thus leaving small pores in the layer. Similar packing has been observed in the atomic force microscopy images of the self-assembled layers of class II hydrophobin, indicating that the crystal structure resembles that of natural hydrophobin film. The orthorhombic crystal structure (1.0 A resolution, R = 13, R(free) = 15) is composed of fiber-like arrays of protein molecules. Rodlet structures have been observed on amphiphilic layers formed by class I hydrophobins; fibrils of class II hydrophobins appear by vigorous shaking. We propose that the structure of the fibrils and/or rodlets is similar to that observed in the crystal structure.
About this Structure
2PL7 is a Single protein structure of sequence from Hypocrea jecorina with and as ligands. Full crystallographic information is available from OCA.
Reference
Crystal structures of hydrophobin HFBII in the presence of detergent implicate the formation of fibrils and monolayer films., Kallio JM, Linder MB, Rouvinen J, J Biol Chem. 2007 Sep 28;282(39):28733-9. Epub 2007 Jul 18. PMID:17636262
Page seeded by OCA on Thu Feb 21 18:30:37 2008
