PDBsum entry 2pl6

Structural protein

PDB id: 2pl6

Contents

Protein chains

(+ 2 more) 71 a.a. *

Ligands

HTG ×3

Waters ×521

* Residue conservation analysis

PDB id:

2pl6

Name:

Structural protein

Title:

Monoclinic crystal structure of hydrophobin hfbii in presence of a detergent

Structure:

Hydrophobin-2. Chain: a, b, c, d, e, f, g, h. Synonym: hydrophobin ii, hfbii

Source:

Hypocrea jecorina. Organism_taxid: 51453

Resolution:

2.20Å R-factor: 0.224 R-free: 0.280

Authors:

J.M.Kallio,J.P.Rouvinen

Key ref:

J.M.Kallio et al. (2007). Crystal Structures of Hydrophobin HFBII in the Presence of Detergent Implicate the Formation of Fibrils and Monolayer Films. J Biol Chem, 282, 28733-28739. PubMed id: 17636262 DOI: 10.1074/jbc.M704238200

Date:

19-Apr-07 Release date: 17-Jul-07

Protein chains

P79073  (HYP2_HYPJE) -  Hydrophobin-2 from Hypocrea jecorina

Seq: 86 a.a.

Struc: 71 a.a.

DOI no: 10.1074/jbc.M704238200

J Biol Chem 282:28733-28739 (2007)

PubMed id: 17636262

Crystal Structures of Hydrophobin HFBII in the Presence of Detergent Implicate the Formation of Fibrils and Monolayer Films.

J.M.Kallio, M.B.Linder, J.Rouvinen.

ABSTRACT

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 (1.0A 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.

Selected figure(s)

Figure 2.
FIGURE 2. The structure of HFBII in space group P2[1]. a, representative electron density of a detergent molecule (red) and the protein (blue). b, the packing of molecules in the asymmetric unit resembles the shape of a horseshoe. c, the formation of a layer structure with alternating hydrophobic and hydrophilic parts is produced by crystal packing (hydrophobic surface areas in red). d, ring-like packing occurs perpendicular to layers.

Figure 5.
FIGURE 5. The mechanism of the function for hydrophobins, schematic representation. Monomers multimerize to dimers, two of which form a tetramer. The tetramer may split into two new dimers with hydrophobic surface areas aligned. These amphiphilic dimers precede the formation of amphiphilic monolayer on hydrophobic-hydrophilic interface. At high concentration, excess hydrophobin forms fibril structures.

The above figures are reprinted by permission from the ASBMB: J Biol Chem (2007, 282, 28733-28739) copyright 2007.

Figures were selected by the author.