This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


2fz6

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2fz6.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2fz6.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2fz6| PDB=2fz6 | SCENE= }}
{{STRUCTURE_2fz6| PDB=2fz6 | SCENE= }}
-
'''Crystal structure of hydrophobin HFBI'''
+
===Crystal structure of hydrophobin HFBI===
-
==Overview==
+
<!--
-
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.
+
The line below this paragraph, {{ABSTRACT_PUBMED_16882996}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 16882996 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_16882996}}
==About this Structure==
==About this Structure==
Line 28: Line 32:
[[Category: Hydrophobin]]
[[Category: Hydrophobin]]
[[Category: Pseudo-merohedral twinning]]
[[Category: Pseudo-merohedral twinning]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 04:29:00 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 15:49:05 2008''

Revision as of 12:49, 29 July 2008

Image:2fz6.png

Template:STRUCTURE 2fz6

Crystal structure of hydrophobin HFBI

Template:ABSTRACT PUBMED 16882996

About this Structure

2FZ6 is a Single protein structure of sequence from Hypocrea jecorina. Full crystallographic information is available from OCA.

Reference

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

Page seeded by OCA on Tue Jul 29 15:49:05 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2fz6"
Personal tools