1r2m: Difference between revisions

Revision as of 19:07, 27 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:1r2m.png

Template:STRUCTURE 1r2m

Atomic resolution structure of the HFBII hydrophobin: a self-assembling amphiphileAtomic resolution structure of the HFBII hydrophobin: a self-assembling amphiphile

Template:ABSTRACT PUBMED 14555650

About this StructureAbout this Structure

1R2M is a Single protein structure of sequence from Hypocrea jecorina. Full crystallographic information is available from OCA.

ReferenceReference

Atomic resolution structure of the HFBII hydrophobin, a self-assembling amphiphile., Hakanpaa J, Paananen A, Askolin S, Nakari-Setala T, Parkkinen T, Penttila M, Linder MB, Rouvinen J, J Biol Chem. 2004 Jan 2;279(1):534-9. Epub 2003 Oct 10. PMID:14555650

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Atomic resolution structure of the HFBII hydrophobin: a self-assembling amphiphile'''
+===Atomic resolution structure of the HFBII hydrophobin: a self-assembling amphiphile===
-==Overview==
+<!--
-Hydrophobins are proteins specific to filamentous fungi. Hydrophobins have several important roles in fungal physiology, for example, adhesion, formation of protective surface coatings, and the reduction of the surface tension of water, which allows growth of aerial structures. Hydrophobins show remarkable biophysical properties, for example, they are the most powerful surface-active proteins known. To this point the molecular basis of the function of this group of proteins has been largely unknown. We have now determined the crystal structure of the hydrophobin HFBII from Trichoderma reesei at 1.0 A resolution. HFBII has a novel, compact single domain structure containing one alpha-helix and four antiparallel beta-strands that completely envelop two disulfide bridges. The protein surface is mainly hydrophilic, but two beta-hairpin loops contain several conserved aliphatic side chains that form a flat hydrophobic patch that makes the molecule amphiphilic. The amphiphilicity of the HFBII molecule is expected to be a source for surface activity, and we suggest that the behavior of this surfactant is greatly enhanced by the self-assembly that is favored by the combination of size and rigidity. This mechanism of function is supported by atomic force micrographs that show highly ordered arrays of HFBII at the air water interface. The data presented show that much of the current views on structure function relations in hydrophobins must be re-evaluated.
+The line below this paragraph, {{ABSTRACT_PUBMED_14555650}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 14555650 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_14555650}}
 ==About this Structure==
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 [[Category: Protein surfactant]]
 [[Category: Self-assembly]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 07:00:04 2008''
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