7vu7: Difference between revisions
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==The Solution structure of the C-terminal domain from flagelliform spidroin== | ==The Solution structure of the C-terminal domain from flagelliform spidroin== | ||
<StructureSection load='7vu7' size='340' side='right'caption='[[7vu7]]' scene=''> | <StructureSection load='7vu7' size='340' side='right'caption='[[7vu7]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full | <table><tr><td colspan='2'>[[7vu7]] is a 2 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7VU7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7VU7 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=7vu7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7vu7 OCA], [https://pdbe.org/7vu7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7vu7 RCSB], [https://www.ebi.ac.uk/pdbsum/7vu7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7vu7 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=7vu7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7vu7 OCA], [https://pdbe.org/7vu7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7vu7 RCSB], [https://www.ebi.ac.uk/pdbsum/7vu7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7vu7 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Spider silk is self-assembled from silk proteins or spidroins. C-terminal domains (CTDs) of various types of spidroins are relatively conserved in amino acid sequences and are suggested to adopt similar structures and perform similar functional roles in spidroin storage and silk formation. Here, we solved the structure of the CTD from a capture-spiral silk protein (CTDFl) and characterized its stability and fibril formation in the presence and absence of a reducing agent at different pH values. CTDFl adopts a dimeric structure with 8 helices, but the CTDs of other types of spidroins exist in a domain-swapped dimeric structure with 10 helices. Despite the structural differences, CTDFl is pH-responsive in stability and fibril formation, similar to the CTDs from minor and major ampullate spidroins. Thus, the functional role of CTDs in silk fiber formation seems conserved. Comparing wild-type CTDFl and its mutants, we found that the pH-responsive behavior results from the protonation of H76, which is conserved from different spider species. In addition, the fibril formation rate of CTDFl correlates with its instability, suggesting that structural changes are involved in fibril formation. | |||
C-Terminal Domains of Spider Silk Proteins Having Divergent Structures but Conserved Functional Roles.,Li X, Fan JS, Shi M, Lai CC, Li J, Meng Q, Yang D Biomacromolecules. 2022 Mar 21. doi: 10.1021/acs.biomac.1c01513. PMID:35312302<ref>PMID:35312302</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7vu7" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Fan | [[Category: Fan, J S]] | ||
[[Category: Yang D]] | [[Category: Yang, D]] | ||
[[Category: Ctd]] | |||
[[Category: Flagelliform spidroin]] | |||
[[Category: Structural protein]] | |||
Revision as of 06:12, 21 April 2022
The Solution structure of the C-terminal domain from flagelliform spidroinThe Solution structure of the C-terminal domain from flagelliform spidroin
Structural highlights
Publication Abstract from PubMedSpider silk is self-assembled from silk proteins or spidroins. C-terminal domains (CTDs) of various types of spidroins are relatively conserved in amino acid sequences and are suggested to adopt similar structures and perform similar functional roles in spidroin storage and silk formation. Here, we solved the structure of the CTD from a capture-spiral silk protein (CTDFl) and characterized its stability and fibril formation in the presence and absence of a reducing agent at different pH values. CTDFl adopts a dimeric structure with 8 helices, but the CTDs of other types of spidroins exist in a domain-swapped dimeric structure with 10 helices. Despite the structural differences, CTDFl is pH-responsive in stability and fibril formation, similar to the CTDs from minor and major ampullate spidroins. Thus, the functional role of CTDs in silk fiber formation seems conserved. Comparing wild-type CTDFl and its mutants, we found that the pH-responsive behavior results from the protonation of H76, which is conserved from different spider species. In addition, the fibril formation rate of CTDFl correlates with its instability, suggesting that structural changes are involved in fibril formation. C-Terminal Domains of Spider Silk Proteins Having Divergent Structures but Conserved Functional Roles.,Li X, Fan JS, Shi M, Lai CC, Li J, Meng Q, Yang D Biomacromolecules. 2022 Mar 21. doi: 10.1021/acs.biomac.1c01513. PMID:35312302[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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