8u9o: Difference between revisions
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==Solution structure of RsgI9 CRE domain from C. thermocellum== | |||
<StructureSection load='8u9o' size='340' side='right'caption='[[8u9o]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8u9o]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Acetivibrio_thermocellus_DSM_1313 Acetivibrio thermocellus DSM 1313]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8U9O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8U9O FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=8u9o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8u9o OCA], [https://pdbe.org/8u9o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8u9o RCSB], [https://www.ebi.ac.uk/pdbsum/8u9o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8u9o ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/RSGI9_ACET2 RSGI9_ACET2] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Clostridium thermocellum is a potential microbial platform to convert abundant plant biomass to biofuels and other renewable chemicals. It efficiently degrades lignocellulosic biomass using a surface displayed cellulosome, a megadalton sized multienzyme containing complex. The enzymatic composition and architecture of the cellulosome is controlled by several transmembrane biomass-sensing RsgI-type anti-sigma factors. Recent studies suggest that these factors transduce signals from the cell surface via a conserved RsgI extracellular (CRE) domain (also called a periplasmic domain) that undergoes autoproteolysis through an incompletely understood mechanism. Here we report the structure of the autoproteolyzed CRE domain from the C. thermocellum RsgI9 anti-sigma factor, revealing that the cleaved fragments forming this domain associate to form a stable alpha/beta/alpha sandwich fold. Based on AlphaFold2 modeling, molecular dynamics simulations, and tandem mass spectrometry, we propose that a conserved Asn-Pro bond in RsgI9 autoproteolyzes via a succinimide intermediate whose formation is promoted by a conserved hydrogen bond network holding the scissile peptide bond in a strained conformation. As other RsgI anti-sigma factors share sequence homology to RsgI9, they likely autoproteolyze through a similar mechanism. | |||
Insight into the autoproteolysis mechanism of the RsgI9 anti-sigma factor from Clostridium thermocellum.,Takayesu A, Mahoney BJ, Goring AK, Jessup T, Ogorzalek Loo RR, Loo JA, Clubb RT Proteins. 2024 Apr 10. doi: 10.1002/prot.26690. PMID:38597224<ref>PMID:38597224</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Clubb | <div class="pdbe-citations 8u9o" style="background-color:#fffaf0;"></div> | ||
[[Category: Mahoney | == References == | ||
[[Category: Takayesu | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Acetivibrio thermocellus DSM 1313]] | |||
[[Category: Large Structures]] | |||
[[Category: Clubb RT]] | |||
[[Category: Mahoney BJ]] | |||
[[Category: Takayesu A]] | |||
Latest revision as of 09:05, 14 July 2024
Solution structure of RsgI9 CRE domain from C. thermocellum
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