4uys: Difference between revisions
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New page: '''Unreleased structure''' The entry 4uys is ON HOLD Authors: Kraushaar, T., Veelders, M., Brueckner, S., Rhinow, D., Moesch, H.U., Essen, L.O. Description: X-ray structure of the N-te... |
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The | ==X-ray structure of the N-terminal domain of the flocculin Flo11 from Saccharomyces cerevisiae== | ||
<StructureSection load='4uys' size='340' side='right'caption='[[4uys]], [[Resolution|resolution]] 1.05Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4uys]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UYS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4UYS FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.05Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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=4uys FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uys OCA], [https://pdbe.org/4uys PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4uys RCSB], [https://www.ebi.ac.uk/pdbsum/4uys PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4uys ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Saccharomyces cerevisiae harbors a family of GPI-anchored cell wall proteins for interaction with its environment. The flocculin Flo11, a major representative of these fungal adhesins, confers formation of different types of multicellular structures such as biofilms, flors, or filaments. To understand these environment-dependent growth phenotypes on a molecular level, we solved the crystal structure of the N-terminal Flo11A domain at 0.89-A resolution. Besides a hydrophobic apical region, the Flo11A domain consists of a beta sandwich of the fibronectin type III domain (FN3). We further show that homophilic Flo11-Flo11 interactions and heterophilic Flo11-plastic interactions solely depend on the Flo11A domain and are strongly pH dependent. These functions of Flo11A involve an apical region with its surface-exposed aromatic band, which is accompanied by acidic stretches. Together with electron microscopic reconstructions of yeast cell-cell contact sites, our data suggest that Flo11 acts as a spacer-like, pH-sensitive adhesin that resembles a membrane-tethered hydrophobin. | |||
Interactions by the Fungal Flo11 Adhesin Depend on a Fibronectin Type III-like Adhesin Domain Girdled by Aromatic Bands.,Kraushaar T, Bruckner S, Veelders M, Rhinow D, Schreiner F, Birke R, Pagenstecher A, Mosch HU, Essen LO Structure. 2015 Jun 2;23(6):1005-17. doi: 10.1016/j.str.2015.03.021. Epub 2015, May 7. PMID:25960408<ref>PMID:25960408</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4uys" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Flocculation protein 3D structures|Flocculation protein 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Saccharomyces cerevisiae S288C]] | |||
[[Category: Brueckner S]] | |||
[[Category: Essen LO]] | |||
[[Category: Kraushaar T]] | |||
[[Category: Moesch HU]] | |||
[[Category: Rhinow D]] | |||
[[Category: Veelders M]] | |||
Latest revision as of 03:36, 21 November 2024
X-ray structure of the N-terminal domain of the flocculin Flo11 from Saccharomyces cerevisiae
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