3vuo: Difference between revisions
New page: '''Unreleased structure''' The entry 3vuo is ON HOLD Authors: Sagane, Y., Miyashita, S.-I., Miyata, K., Matsumoto, T., Inui, K., Hayashi, S., Suzuki, T., Hasegawa, K., Yajima, S., Yaman... |
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The | ==Crystal structure of nontoxic nonhemagglutinin subcomponent (NTNHA) from clostridium botulinum serotype D strain 4947== | ||
<StructureSection load='3vuo' size='340' side='right'caption='[[3vuo]], [[Resolution|resolution]] 3.90Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3vuo]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_botulinus"_van_ermengem_1896 "bacillus botulinus" van ermengem 1896]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VUO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VUO FirstGlance]. <br> | |||
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ntnha ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1491 "Bacillus botulinus" van Ermengem 1896])</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=3vuo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vuo OCA], [https://pdbe.org/3vuo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vuo RCSB], [https://www.ebi.ac.uk/pdbsum/3vuo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vuo ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
In cell culture supernatants, the botulinum neurotoxin (BoNT) exists as part of a toxin complex (TC) in which nontoxic nonhemagglutinin (NTNHA) and/or hemagglutinins (HAs) are assembled onto the BoNT. A series of investigations indicated that formation of the TC is vital for delivery of the toxin to nerve cells through the digestive tract. In the assembly process, BoNT binds to NTNHA yielding M-TC, and it then matures into L-TC by further association with the HAs via NTNHA in the M-TC. Here, we report a crystal structure of the NTNHA from Clostridium botulinum serotype D strain 4947. Additionally, we performed small-angle X-ray scattering (SAXS) analysis of the NTNHA and the M-TC to elucidate the solution structure. The crystal structure of D-4947 NTNHA revealed that BoNT and NTNHA share a closely related structure consisting of three domains. The SAXS image indicated that, even though the N-terminal two-thirds of the NTNHA molecule had an apparently similar conformation in both the crystal and solution structures, the C-terminal third of the molecule showed a more extended structure in the SAXS image than that seen in the crystallographic image. The discrepancy between the crystal and solution structures implies a high flexibility of the C-terminal third domain of NTNHA, which is involved in binding to BoNT. Structural dynamics of the NTNHA molecule revealed by SAXS may explain its binding to BoNT to form the BoNT/NTNHA complex. | |||
Small-angle X-ray scattering reveals structural dynamics of the botulinum neurotoxin associating protein, nontoxic nonhemagglutinin.,Sagane Y, Miyashita S, Miyata K, Matsumoto T, Inui K, Hayashi S, Suzuki T, Hasegawa K, Yajima S, Yamano A, Niwa K, Watanabe T Biochem Biophys Res Commun. 2012 Aug 24;425(2):256-60. Epub 2012 Jul 22. PMID:22828508<ref>PMID:22828508</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3vuo" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Bacillus botulinus van ermengem 1896]] | |||
[[Category: Large Structures]] | |||
[[Category: Hasegawa, K]] | |||
[[Category: Hayashi, S]] | |||
[[Category: Inui, K]] | |||
[[Category: Matsumoto, T]] | |||
[[Category: Miyashita, S I]] | |||
[[Category: Miyata, K]] | |||
[[Category: Niwa, K]] | |||
[[Category: Sagane, Y]] | |||
[[Category: Suzuki, T]] | |||
[[Category: Watanabe, T]] | |||
[[Category: Yajima, S]] | |||
[[Category: Yamano, A]] | |||
[[Category: Botulinum neurotoxin]] | |||
[[Category: Protection of botulinum neurotoxin]] | |||
[[Category: Toxin]] | |||
Latest revision as of 22:04, 27 July 2022
Crystal structure of nontoxic nonhemagglutinin subcomponent (NTNHA) from clostridium botulinum serotype D strain 4947Crystal structure of nontoxic nonhemagglutinin subcomponent (NTNHA) from clostridium botulinum serotype D strain 4947
Structural highlights
Publication Abstract from PubMedIn cell culture supernatants, the botulinum neurotoxin (BoNT) exists as part of a toxin complex (TC) in which nontoxic nonhemagglutinin (NTNHA) and/or hemagglutinins (HAs) are assembled onto the BoNT. A series of investigations indicated that formation of the TC is vital for delivery of the toxin to nerve cells through the digestive tract. In the assembly process, BoNT binds to NTNHA yielding M-TC, and it then matures into L-TC by further association with the HAs via NTNHA in the M-TC. Here, we report a crystal structure of the NTNHA from Clostridium botulinum serotype D strain 4947. Additionally, we performed small-angle X-ray scattering (SAXS) analysis of the NTNHA and the M-TC to elucidate the solution structure. The crystal structure of D-4947 NTNHA revealed that BoNT and NTNHA share a closely related structure consisting of three domains. The SAXS image indicated that, even though the N-terminal two-thirds of the NTNHA molecule had an apparently similar conformation in both the crystal and solution structures, the C-terminal third of the molecule showed a more extended structure in the SAXS image than that seen in the crystallographic image. The discrepancy between the crystal and solution structures implies a high flexibility of the C-terminal third domain of NTNHA, which is involved in binding to BoNT. Structural dynamics of the NTNHA molecule revealed by SAXS may explain its binding to BoNT to form the BoNT/NTNHA complex. Small-angle X-ray scattering reveals structural dynamics of the botulinum neurotoxin associating protein, nontoxic nonhemagglutinin.,Sagane Y, Miyashita S, Miyata K, Matsumoto T, Inui K, Hayashi S, Suzuki T, Hasegawa K, Yajima S, Yamano A, Niwa K, Watanabe T Biochem Biophys Res Commun. 2012 Aug 24;425(2):256-60. Epub 2012 Jul 22. PMID:22828508[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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