4uyt: Difference between revisions
New page: '''Unreleased structure''' The entry 4uyt 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='4uyt' size='340' side='right'caption='[[4uyt]], [[Resolution|resolution]] 1.03Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4uyt]] 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=4UYT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4UYT 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]] 1.03Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</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=4uyt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uyt OCA], [https://pdbe.org/4uyt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4uyt RCSB], [https://www.ebi.ac.uk/pdbsum/4uyt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4uyt ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/FLO11_YEAST FLO11_YEAST] Cell wall protein that participates in adhesive cell-cell interactions during yeast flocculation, a reversible, asexual and Ca(2+)-dependent process in which cells adhere to form aggregates (flocs) consisting of thousands of cells. Also involved in cell-substrate adhesion, haploid invasive growth, diploid pseudohyphae formation and biofilm (flor) development. The precise mechanism by which this protein mediates adhesion is unclear but may involve homotypic binding. Adhesive activity is inhibited by mannose, but not by glucose, maltose, sucrose or galactose.<ref>PMID:11027318</ref> <ref>PMID:11157168</ref> <ref>PMID:16043420</ref> <ref>PMID:17921350</ref> <ref>PMID:18001350</ref> <ref>PMID:20619652</ref> <ref>PMID:22129043</ref> <ref>PMID:8710886</ref> <ref>PMID:8955395</ref> | |||
<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 4uyt" 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]] | |||