7c7u: Difference between revisions
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7c7u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7c7u OCA], [https://pdbe.org/7c7u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7c7u RCSB], [https://www.ebi.ac.uk/pdbsum/7c7u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7c7u ProSAT]</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=7c7u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7c7u OCA], [https://pdbe.org/7c7u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7c7u RCSB], [https://www.ebi.ac.uk/pdbsum/7c7u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7c7u ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The Staphylococcal Bap proteins sense environmental signals (such as pH, [Ca(2+) ]) to build amyloid scaffold biofilm matrices via unknown mechanisms. We here report the crystal structure of the aggregation-prone region of Staphylococcus aureus Bap which adopts a dumbbell-shaped fold. The middle module (MM) connecting the N-terminal and C-terminal lobes consists of a tandem of novel double-Ca(2+) -binding motifs involved in cooperative interaction networks, which undergoes Ca(2+) -dependent order-disorder conformational switches. The N-terminal lobe is sufficient to mediate amyloid aggregation through liquid-liquid phase separation and maturation, and subsequent biofilm formation under acidic conditions. Such processes are promoted by disordered MM at low [Ca(2+) ] but inhibited by ordered MM stabilized by Ca(2+) binding, with inhibition efficiency depending on structural integrity of the interaction networks. These studies illustrate a novel protein switch in pathogenic bacteria and provide insights into the mechanistic understanding of Bap proteins in modulation of functional amyloid and biofilm formation, which could be implemented in the anti-biofilm drug design. | |||
Structural mechanism for modulation of functional amyloid and biofilm formation by Staphylococcal Bap protein switch.,Ma J, Cheng X, Xu Z, Zhang Y, Valle J, Fan S, Zuo X, Lasa I, Fang X EMBO J. 2021 May 28:e107500. doi: 10.15252/embj.2020107500. PMID:34046916<ref>PMID:34046916</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7c7u" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 15:31, 9 June 2021
Biofilm associated protein - BSP domainBiofilm associated protein - BSP domain
Structural highlights
Publication Abstract from PubMedThe Staphylococcal Bap proteins sense environmental signals (such as pH, [Ca(2+) ]) to build amyloid scaffold biofilm matrices via unknown mechanisms. We here report the crystal structure of the aggregation-prone region of Staphylococcus aureus Bap which adopts a dumbbell-shaped fold. The middle module (MM) connecting the N-terminal and C-terminal lobes consists of a tandem of novel double-Ca(2+) -binding motifs involved in cooperative interaction networks, which undergoes Ca(2+) -dependent order-disorder conformational switches. The N-terminal lobe is sufficient to mediate amyloid aggregation through liquid-liquid phase separation and maturation, and subsequent biofilm formation under acidic conditions. Such processes are promoted by disordered MM at low [Ca(2+) ] but inhibited by ordered MM stabilized by Ca(2+) binding, with inhibition efficiency depending on structural integrity of the interaction networks. These studies illustrate a novel protein switch in pathogenic bacteria and provide insights into the mechanistic understanding of Bap proteins in modulation of functional amyloid and biofilm formation, which could be implemented in the anti-biofilm drug design. Structural mechanism for modulation of functional amyloid and biofilm formation by Staphylococcal Bap protein switch.,Ma J, Cheng X, Xu Z, Zhang Y, Valle J, Fan S, Zuo X, Lasa I, Fang X EMBO J. 2021 May 28:e107500. doi: 10.15252/embj.2020107500. PMID:34046916[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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