2fmc: Difference between revisions

Revision as of 04:45, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2fmc.png

Template:STRUCTURE 2fmc

Solution structure of the class I hydrophobin EASSolution structure of the class I hydrophobin EAS

Template:ABSTRACT PUBMED 16537446

About this StructureAbout this Structure

2FMC is a Single protein structure of sequence from Neurospora crassa. Full experimental 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

Page seeded by OCA on Mon Jul 28 04:45:12 2008

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OCA

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-[[Image:2fmc.gif|left|200px]]
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 {{STRUCTURE_2fmc|  PDB=2fmc  |  SCENE=  }}
-'''Solution structure of the class I hydrophobin EAS'''
+===Solution structure of the class I hydrophobin EAS===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_16537446}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16537446 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_16537446}}
 ==About this Structure==
-FMC is a [[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].
+FMC is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Neurospora_crassa Neurospora crassa]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FMC OCA].
 ==Reference==
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 [[Category: Disulphide bond]]
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