4uyr

From Proteopedia

(Difference between revisions)

Current revision

X-ray structure of the N-terminal domain of the flocculin Flo11 from Saccharomyces cerevisiae

Structural highlights

4uyr is a 1 chain structure with sequence from Saccharomyces cerevisiae S288C. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 0.89Å
Ligands:	, ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.^[1] ^[2] ^[3] ^[4] ^[5] ^[6] ^[7] ^[8] ^[9]

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^[10]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Guo B, Styles CA, Feng Q, Fink GR. A Saccharomyces gene family involved in invasive growth, cell-cell adhesion, and mating. Proc Natl Acad Sci U S A. 2000 Oct 24;97(22):12158-63. PMID:11027318 doi:http://dx.doi.org/10.1073/pnas.220420397
↑ Reynolds TB, Fink GR. Bakers' yeast, a model for fungal biofilm formation. Science. 2001 Feb 2;291(5505):878-81. PMID:11157168 doi:http://dx.doi.org/10.1126/science.291.5505.878
↑ Bayly JC, Douglas LM, Pretorius IS, Bauer FF, Dranginis AM. Characteristics of Flo11-dependent flocculation in Saccharomyces cerevisiae. FEMS Yeast Res. 2005 Dec;5(12):1151-6. Epub 2005 Jul 1. PMID:16043420 doi:http://dx.doi.org/S1567-1356(05)00100-5
↑ Douglas LM, Li L, Yang Y, Dranginis AM. Expression and characterization of the flocculin Flo11/Muc1, a Saccharomyces cerevisiae mannoprotein with homotypic properties of adhesion. Eukaryot Cell. 2007 Dec;6(12):2214-21. Epub 2007 Oct 5. PMID:17921350 doi:http://dx.doi.org/EC.00284-06
↑ Fichtner L, Schulze F, Braus GH. Differential Flo8p-dependent regulation of FLO1 and FLO11 for cell-cell and cell-substrate adherence of S. cerevisiae S288c. Mol Microbiol. 2007 Dec;66(5):1276-89. PMID:18001350 doi:http://dx.doi.org/MMI6014
↑ Karunanithi S, Vadaie N, Chavel CA, Birkaya B, Joshi J, Grell L, Cullen PJ. Shedding of the mucin-like flocculin Flo11p reveals a new aspect of fungal adhesion regulation. Curr Biol. 2010 Aug 10;20(15):1389-95. doi: 10.1016/j.cub.2010.06.033. Epub 2010 , Jul 8. PMID:20619652 doi:http://dx.doi.org/10.1016/j.cub.2010.06.033
↑ Goossens KV, Willaert RG. The N-terminal domain of the Flo11 protein from Saccharomyces cerevisiae is an adhesin without mannose-binding activity. FEMS Yeast Res. 2012 Feb;12(1):78-87. doi: 10.1111/j.1567-1364.2011.00766.x. Epub, 2011 Dec 22. PMID:22129043 doi:http://dx.doi.org/10.1111/j.1567-1364.2011.00766.x
↑ Lambrechts MG, Bauer FF, Marmur J, Pretorius IS. Muc1, a mucin-like protein that is regulated by Mss10, is critical for pseudohyphal differentiation in yeast. Proc Natl Acad Sci U S A. 1996 Aug 6;93(16):8419-24. PMID:8710886
↑ Lo WS, Dranginis AM. FLO11, a yeast gene related to the STA genes, encodes a novel cell surface flocculin. J Bacteriol. 1996 Dec;178(24):7144-51. PMID:8955395
↑ Kraushaar T, Bruckner S, Veelders M, Rhinow D, Schreiner F, Birke R, Pagenstecher A, Mosch HU, Essen LO. Interactions by the Fungal Flo11 Adhesin Depend on a Fibronectin Type III-like Adhesin Domain Girdled by Aromatic Bands. Structure. 2015 Jun 2;23(6):1005-17. doi: 10.1016/j.str.2015.03.021. Epub 2015, May 7. PMID:25960408 doi:http://dx.doi.org/10.1016/j.str.2015.03.021

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4uyr"

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 == Structural highlights ==
 <table><tr><td colspan='2'>[[4uyr]] 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=4UYR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4UYR FirstGlance]. <br>
-</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>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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]] 0.89&#8491;</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>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=4uyr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uyr OCA], [https://pdbe.org/4uyr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4uyr RCSB], [https://www.ebi.ac.uk/pdbsum/4uyr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4uyr ProSAT]</span></td></tr>
 </table>

4uyr

From Proteopedia

Current revision

X-ray structure of the N-terminal domain of the flocculin Flo11 from Saccharomyces cerevisiae

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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