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| | <StructureSection load='2pl6' size='340' side='right'caption='[[2pl6]], [[Resolution|resolution]] 2.20Å' scene=''> | | <StructureSection load='2pl6' size='340' side='right'caption='[[2pl6]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2pl6]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Hypocrea_jecorina Hypocrea jecorina]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PL6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PL6 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2pl6]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Trichoderma_reesei Trichoderma reesei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PL6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PL6 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HTG:HEPTYL+1-THIOHEXOPYRANOSIDE'>HTG</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1r2m|1r2m]], [[2b97|2b97]], [[2fz6|2fz6]], [[2gvm|2gvm]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HTG:HEPTYL+1-THIOHEXOPYRANOSIDE'>HTG</scene></td></tr> |
| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2pl6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pl6 OCA], [https://pdbe.org/2pl6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2pl6 RCSB], [https://www.ebi.ac.uk/pdbsum/2pl6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2pl6 ProSAT]</span></td></tr> | | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2pl6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pl6 OCA], [https://pdbe.org/2pl6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2pl6 RCSB], [https://www.ebi.ac.uk/pdbsum/2pl6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2pl6 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/HYP2_HYPJE HYP2_HYPJE]] Responsible for spore hydrophobicity and protection.
| + | [https://www.uniprot.org/uniprot/HYP2_HYPJE HYP2_HYPJE] Responsible for spore hydrophobicity and protection. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Hypocrea jecorina]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Kallio, J M]] | + | [[Category: Trichoderma reesei]] |
| - | [[Category: Rouvinen, J P]] | + | [[Category: Kallio JM]] |
| - | [[Category: Amphiphile]] | + | [[Category: Rouvinen JP]] |
| - | [[Category: Hydrophobin]]
| + | |
| - | [[Category: Protein surfactant]]
| + | |
| - | [[Category: Structural protein]]
| + | |
| Structural highlights
Function
HYP2_HYPJE Responsible for spore hydrophobicity and protection.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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 (1.0 A 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.
Crystal structures of hydrophobin HFBII in the presence of detergent implicate the formation of fibrils and monolayer films.,Kallio JM, Linder MB, Rouvinen J J Biol Chem. 2007 Sep 28;282(39):28733-9. Epub 2007 Jul 18. PMID:17636262[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kallio JM, Linder MB, Rouvinen J. Crystal structures of hydrophobin HFBII in the presence of detergent implicate the formation of fibrils and monolayer films. J Biol Chem. 2007 Sep 28;282(39):28733-9. Epub 2007 Jul 18. PMID:17636262 doi:10.1074/jbc.M704238200
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