6lci: Difference between revisions

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==Solution structure of mdaA-1 domain==
==Solution structure of mdaA-1 domain==
<StructureSection load='6lci' size='340' side='right'caption='[[6lci]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
<StructureSection load='6lci' size='340' side='right'caption='[[6lci]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6lci]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/As_rm_7_[[rhizomucor_regularior]] As rm 7 [[rhizomucor regularior]]]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6LCI OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6LCI FirstGlance]. <br>
<table><tr><td colspan='2'>[[6lci]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mucor_circinelloides Mucor circinelloides]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6LCI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6LCI FirstGlance]. <br>
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6lci FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6lci OCA], [http://pdbe.org/6lci PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6lci RCSB], [http://www.ebi.ac.uk/pdbsum/6lci PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6lci ProSAT]</span></td></tr>
</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=6lci FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6lci OCA], [https://pdbe.org/6lci PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6lci RCSB], [https://www.ebi.ac.uk/pdbsum/6lci PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6lci ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/S2JLE7_MUCC1 S2JLE7_MUCC1]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Multicellular organisms employ fluid transport networks to overcome the limit of diffusion and promote essential long-distance transport. Connectivity and pressurization render these networks especially vulnerable to wounding. To mitigate this risk, animals, plants, and multicellular fungi independently evolved elaborate clotting and plugging mechanisms. In the septate filamentous fungi, membrane-bound organelles plug septal pores in wounded hyphae. By contrast, vegetative hyphae in the early-diverging Mucoromycota are largely aseptate, and how their hyphae respond to wounding is unknown. Here, we show that wounding in the Mucorales leads to explosive protoplasmic discharge that is rapidly terminated by protoplasmic gelation. We identify Mucoromycota-specific Gellin proteins, whose loss of function leads to uncontrolled wound-induced protoplasmic bleeding. Gellins contain ten related beta-trefoil Gll domains, each of which possesses unique features that impart distinct gelation-related properties: some readily unfold and form high-order sheet-like structures when subjected to mechanical force from flow, while others possess hydrophobic motifs that enable membrane binding. In cell-free reconstitution, sheet-like structures formed by a partial Gellin incorporate membranous organelles. Together, these data define a mechanistic basis for regulated protoplasmic gelation, and provide new design principles for the development of artificial flow-responsive biomaterials.
Fungal Wound Healing through Instantaneous Protoplasmic Gelation.,Nguyen TA, Le S, Lee M, Fan JS, Yang D, Yan J, Jedd G Curr Biol. 2021 Jan 25;31(2):271-282.e5. doi: 10.1016/j.cub.2020.10.016. Epub , 2020 Nov 12. PMID:33186551<ref>PMID:33186551</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6lci" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Fan, J S]]
[[Category: Mucor circinelloides]]
[[Category: Jedd, G]]
[[Category: Fan JS]]
[[Category: Le, S]]
[[Category: Jedd G]]
[[Category: Lee, M]]
[[Category: Le S]]
[[Category: Nguyen, T A]]
[[Category: Lee M]]
[[Category: Yan, J]]
[[Category: Nguyen TA]]
[[Category: Yang, D]]
[[Category: Yan J]]
[[Category: Cytoplasmic phase transition]]
[[Category: Yang D]]
[[Category: Flow-induced aggregation]]
[[Category: Structural protein]]
[[Category: Wound healing]]

Latest revision as of 13:54, 14 June 2023

Solution structure of mdaA-1 domainSolution structure of mdaA-1 domain

Structural highlights

6lci is a 1 chain structure with sequence from Mucor circinelloides. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

S2JLE7_MUCC1

Publication Abstract from PubMed

Multicellular organisms employ fluid transport networks to overcome the limit of diffusion and promote essential long-distance transport. Connectivity and pressurization render these networks especially vulnerable to wounding. To mitigate this risk, animals, plants, and multicellular fungi independently evolved elaborate clotting and plugging mechanisms. In the septate filamentous fungi, membrane-bound organelles plug septal pores in wounded hyphae. By contrast, vegetative hyphae in the early-diverging Mucoromycota are largely aseptate, and how their hyphae respond to wounding is unknown. Here, we show that wounding in the Mucorales leads to explosive protoplasmic discharge that is rapidly terminated by protoplasmic gelation. We identify Mucoromycota-specific Gellin proteins, whose loss of function leads to uncontrolled wound-induced protoplasmic bleeding. Gellins contain ten related beta-trefoil Gll domains, each of which possesses unique features that impart distinct gelation-related properties: some readily unfold and form high-order sheet-like structures when subjected to mechanical force from flow, while others possess hydrophobic motifs that enable membrane binding. In cell-free reconstitution, sheet-like structures formed by a partial Gellin incorporate membranous organelles. Together, these data define a mechanistic basis for regulated protoplasmic gelation, and provide new design principles for the development of artificial flow-responsive biomaterials.

Fungal Wound Healing through Instantaneous Protoplasmic Gelation.,Nguyen TA, Le S, Lee M, Fan JS, Yang D, Yan J, Jedd G Curr Biol. 2021 Jan 25;31(2):271-282.e5. doi: 10.1016/j.cub.2020.10.016. Epub , 2020 Nov 12. PMID:33186551[1]

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

References

  1. Nguyen TA, Le S, Lee M, Fan JS, Yang D, Yan J, Jedd G. Fungal Wound Healing through Instantaneous Protoplasmic Gelation. Curr Biol. 2021 Jan 25;31(2):271-282.e5. PMID:33186551 doi:10.1016/j.cub.2020.10.016
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