2fmc: Difference between revisions
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'''Solution structure of the class I hydrophobin EAS'''<br /> | '''Solution structure of the class I hydrophobin EAS'''<br /> | ||
==Overview== | ==Overview== | ||
Class I hydrophobins are a unique family of fungal proteins that form a | Class I hydrophobins are a unique family of fungal proteins that form a polymeric, water-repellent monolayer on the surface of structures such as spores and fruiting bodies. Similar monolayers are being discovered on an increasing range of important microorganisms. Hydrophobin monolayers are amphipathic and particularly robust, and they reverse the wettability of the surface on which they are formed. There are also significant similarities between these polymers and amyloid-like fibrils. However, structural information on these proteins and the rodlets they form has been elusive. Here, we describe the three-dimensional structure of the monomeric form of the class I hydrophobin EAS. EAS forms a beta-barrel structure punctuated by several disordered regions and displays a complete segregation of charged and hydrophobic residues on its surface. This structure is consistent with its ability to form an amphipathic polymer. By using this structure, together with data from mutagenesis and previous biophysical studies, we have been able to propose a model for the polymeric rodlet structure adopted by these proteins. X-ray fiber diffraction data from EAS rodlets are consistent with our model. Our data provide molecular insight into the nature of hydrophobin rodlet films and extend our understanding of the fibrillar beta-structures that continue to be discovered in the protein world. | ||
==About this Structure== | ==About this Structure== | ||
2FMC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Neurospora_crassa Neurospora crassa]. Full crystallographic information is available from [http:// | 2FMC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Neurospora_crassa Neurospora crassa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FMC OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Neurospora crassa]] | [[Category: Neurospora crassa]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Kwan, A | [[Category: Kwan, A H.]] | ||
[[Category: beta barrel]] | [[Category: beta barrel]] | ||
[[Category: disulphide bonds]] | [[Category: disulphide bonds]] | ||
[[Category: flexible loop]] | [[Category: flexible loop]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:23:00 2008'' | ||
Revision as of 18:23, 21 February 2008
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Solution structure of the class I hydrophobin EAS
OverviewOverview
Class I hydrophobins are a unique family of fungal proteins that form a polymeric, water-repellent monolayer on the surface of structures such as spores and fruiting bodies. Similar monolayers are being discovered on an increasing range of important microorganisms. Hydrophobin monolayers are amphipathic and particularly robust, and they reverse the wettability of the surface on which they are formed. There are also significant similarities between these polymers and amyloid-like fibrils. However, structural information on these proteins and the rodlets they form has been elusive. Here, we describe the three-dimensional structure of the monomeric form of the class I hydrophobin EAS. EAS forms a beta-barrel structure punctuated by several disordered regions and displays a complete segregation of charged and hydrophobic residues on its surface. This structure is consistent with its ability to form an amphipathic polymer. By using this structure, together with data from mutagenesis and previous biophysical studies, we have been able to propose a model for the polymeric rodlet structure adopted by these proteins. X-ray fiber diffraction data from EAS rodlets are consistent with our model. Our data provide molecular insight into the nature of hydrophobin rodlet films and extend our understanding of the fibrillar beta-structures that continue to be discovered in the protein world.
About this StructureAbout this Structure
2FMC is a Single protein structure of sequence from Neurospora crassa. Full crystallographic information is available from OCA.
ReferenceReference
Structural basis for rodlet assembly in fungal hydrophobins., Kwan AH, Winefield RD, Sunde M, Matthews JM, Haverkamp RG, Templeton MD, Mackay JP, Proc Natl Acad Sci U S A. 2006 Mar 7;103(10):3621-6. Epub 2006 Feb 28. PMID:16537446
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