4uyt: Difference between revisions

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 ==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]] 1.03&Aring;' scene=''>
+<StructureSection load='4uyt' size='340' side='right'caption='[[4uyt]], [[Resolution|resolution]] 1.03&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4uyt]] is a 1 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4UYT FirstGlance]. <br>
+<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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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]] 1.03&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4uyr|4uyr]], [[4uys|4uys]]</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4uyt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uyt OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4uyt RCSB], [http://www.ebi.ac.uk/pdbsum/4uyt PDBsum]</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=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 ==
-[[http://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>
+[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 ==
@@ Line 17: / Line 18: @@
 From MEDLINE&reg;/PubMed&reg;, 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: Brueckner, S]]
+[[Category: Large Structures]]
-[[Category: Essen, L O]]
+[[Category: Saccharomyces cerevisiae S288C]]
-[[Category: Kraushaar, T]]
+[[Category: Brueckner S]]
-[[Category: Moesch, H U]]
+[[Category: Essen LO]]
-[[Category: Rhinow, D]]
+[[Category: Kraushaar T]]
-[[Category: Veelders, M]]
+[[Category: Moesch HU]]
-[[Category: Adhesin]]
+[[Category: Rhinow D]]
-[[Category: Cell adhesion]]
+[[Category: Veelders M]]
-[[Category: Flocculation]]
-[[Category: Homotypic binding]]
-[[Category: Hydrophobic patch]]