2rsx: Difference between revisions
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==Solution structure of IseA, an inhibitor protein of DL-endopeptidases from Bacillus subtilis== | ==Solution structure of IseA, an inhibitor protein of DL-endopeptidases from Bacillus subtilis== | ||
<StructureSection load='2rsx' size='340' side='right'caption='[[2rsx | <StructureSection load='2rsx' size='340' side='right'caption='[[2rsx]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2rsx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[2rsx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis_subsp._subtilis_str._168 Bacillus subtilis subsp. subtilis str. 168]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RSX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RSX FirstGlance]. <br> | ||
</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=2rsx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rsx OCA], [https://pdbe.org/2rsx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rsx RCSB], [https://www.ebi.ac.uk/pdbsum/2rsx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rsx ProSAT]</span></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=2rsx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rsx OCA], [https://pdbe.org/2rsx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rsx RCSB], [https://www.ebi.ac.uk/pdbsum/2rsx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rsx ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/YOEB_BACSU YOEB_BACSU] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Bacillus subtilis subsp. subtilis str. 168]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Arai | [[Category: Arai R]] | ||
[[Category: Fukui | [[Category: Fukui S]] | ||
[[Category: Kigawa | [[Category: Kigawa T]] | ||
[[Category: Kitaura | [[Category: Kitaura C]] | ||
[[Category: Kobayashi | [[Category: Kobayashi N]] | ||
[[Category: Li | [[Category: Li H]] | ||
[[Category: Sekiguchi | [[Category: Sekiguchi J]] | ||
[[Category: Tochio | [[Category: Tochio N]] | ||
[[Category: Watanabe | [[Category: Watanabe S]] | ||
Latest revision as of 23:52, 12 April 2023
Solution structure of IseA, an inhibitor protein of DL-endopeptidases from Bacillus subtilisSolution structure of IseA, an inhibitor protein of DL-endopeptidases from Bacillus subtilis
Structural highlights
FunctionPublication Abstract from PubMedIn Bacillus subtilis, LytE, LytF, CwlS, and CwlO are vegetative autolysins, dl-endopeptidases in the NlpC/P60 family, and play essential roles in cell growth and separation. IseA (YoeB) is a proteinaceous inhibitor against the dl-endopeptidases, peptidoglycan hydrolases. Overexpression of IseA caused significantly long chained cell morphology, because IseA inhibits the cell separation dl-endopeptidases post-translationally. Here, we report the first three-dimensional structure of IseA, determined by NMR spectroscopy. The structure includes a single domain consisting of three alpha-helices, one 3(10)-helix, and eight beta-strands, which is a novel fold like a "hacksaw." Noteworthy is a dynamic loop between beta4 and the 3(10)-helix, which resembles a "blade." The electrostatic potential distribution shows that most of the surface is positively charged, but the region around the loop is negatively charged. In contrast, the LytF active-site cleft is expected to be positively charged. NMR chemical shift perturbation of IseA interacting with LytF indicated that potential interaction sites are located around the loop. Furthermore, the IseA mutants D100K/D102K and G99P/G101P at the loop showed dramatic loss of inhibition activity against LytF, compared with wild-type IseA, indicating that the beta4-3(10) loop plays an important role in inhibition. Moreover, we built a complex structure model of IseA-LytF by docking simulation, suggesting that the beta4-3(10) loop of IseA gets stuck deep in the cleft of LytF, and the active site is occluded. These results suggest a novel inhibition mechanism of the hacksaw-like structure, which is different from known inhibitor proteins, through interactions around the characteristic loop regions with the active-site cleft of enzymes. Solution Structure of IseA, an Inhibitor Protein of DL-Endopeptidases from Bacillus subtilis, Reveals a Novel Fold with a Characteristic Inhibitory Loop.,Arai R, Fukui S, Kobayashi N, Sekiguchi J J Biol Chem. 2012 Dec 28;287(53):44736-48. doi: 10.1074/jbc.M112.414763. Epub, 2012 Oct 22. PMID:23091053[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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