Flocculation protein
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
| - | The N-terminal domain of FLO is similar to the lectin-like domain of [[Adhesin]]. | + | The N-terminal domain of FLO is similar to the lectin-like domain of [[Adhesin]]. The Ca+2 ion binds to two carbohydrate-binding groups: a D''cis''D motif - 2 Asp residues connected with a ''cis'' bond and another β strand residues. The Ca+2 ion interacts with α-mannose which is an antiflocculant in vivo<ref>PMID:21149680</ref>. <scene name='91/919029/Cv/7'>α-mannose binding site</scene>. |
==3D structures of flocculation protein== | ==3D structures of flocculation protein== | ||
[[Flocculation protein 3D structures]] | [[Flocculation protein 3D structures]] | ||
Revision as of 12:17, 6 September 2022
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References
- ↑ Goossens K, Willaert R. Flocculation protein structure and cell-cell adhesion mechanism in Saccharomyces cerevisiae. Biotechnol Lett. 2010 Nov;32(11):1571-85. doi: 10.1007/s10529-010-0352-3. Epub, 2010 Jul 18. PMID:20640875 doi:http://dx.doi.org/10.1007/s10529-010-0352-3
- ↑ Verstrepen KJ, Derdelinckx G, Verachtert H, Delvaux FR. Yeast flocculation: what brewers should know. Appl Microbiol Biotechnol. 2003 May;61(3):197-205. doi:, 10.1007/s00253-002-1200-8. Epub 2003 Jan 25. PMID:12698276 doi:http://dx.doi.org/10.1007/s00253-002-1200-8
- ↑ Veelders M, Bruckner S, Ott D, Unverzagt C, Mosch HU, Essen LO. Structural basis of flocculin-mediated social behavior in yeast. Proc Natl Acad Sci U S A. 2010 Dec 28;107(52):22511-6. Epub 2010 Dec 13. PMID:21149680 doi:10.1073/pnas.1013210108
