View source for 8i2f


==Crystal structure of Bacillus subtilis LytE catalytic domain in complex with IseA==
<StructureSection load='8i2f' size='340' side='right'caption='[[8i2f]], [[Resolution|resolution]] 2.03&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8i2f]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis_subsp._subtilis_str._168 Bacillus subtilis subsp. subtilis str. 168]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8I2F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8I2F 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=8i2f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8i2f OCA], [https://pdbe.org/8i2f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8i2f RCSB], [https://www.ebi.ac.uk/pdbsum/8i2f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8i2f ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/YOEB_BACSU YOEB_BACSU] 
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== Publication Abstract from PubMed ==
Peptidoglycan, a physical barrier that protects bacteria from the environment, is constantly degraded and resynthesized for remodeling during cell growth and division. Because excessive or insufficient peptidoglycan hydrolysis affects bacterial homeostasis and viability, peptidoglycan degradation must be precisely regulated. In Bacillus subtilis, DL-endopeptidases play an essential role in peptidoglycan remodeling, and their activity is regulated by IseA. Here, we report the crystal structure of peptidoglycan DL-endopeptidase LytE complexed with IseA. In the crystal structure, the inhibitory loop connecting the two lobes of IseA blocks the active site of LytE by mimicking its substrate. Consistently, mutations in the inhibitory loop resulted in the loss of IseA activity. The structure also shows that conformational rearrangements in both LytE and IseA restrict access of the inhibitory loop to the LytE catalytic site. These results reveal an inhibition mechanism of peptidoglycan DL-endopeptidase in which the inhibitory protein mimics the substrate but is not degraded.

Structural insights into the regulation of peptidoglycan DL-endopeptidases by inhibitory protein IseA.,Tandukar S, Kwon E, Kim DY Structure. 2023 Mar 11:S0969-2126(23)00075-8. doi: 10.1016/j.str.2023.02.013. PMID:36963396<ref>PMID:36963396</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 8i2f" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Bacillus subtilis subsp. subtilis str. 168]]
[[Category: Large Structures]]
[[Category: Kim DY]]
[[Category: Kwon E]]
[[Category: Tandukar S]]