6lci: Difference between revisions

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-'''Unreleased structure'''
-The entry 6lci is ON HOLD
+==Solution structure of mdaA-1 domain==
+<StructureSection load='6lci' size='340' side='right'caption='[[6lci]]' scene=''>
+== Structural highlights ==
+<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'>[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>
+== 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.
-Authors:
+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>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 6lci" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Mucor circinelloides]]
+[[Category: Fan JS]]
+[[Category: Jedd G]]
+[[Category: Le S]]
+[[Category: Lee M]]
+[[Category: Nguyen TA]]
+[[Category: Yan J]]
+[[Category: Yang D]]