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| | ==Crystal structure of the Bacillus cereus spore cortex-lytic enzyme SleL== | | ==Crystal structure of the Bacillus cereus spore cortex-lytic enzyme SleL== |
| - | <StructureSection load='4s3j' size='340' side='right' caption='[[4s3j]], [[Resolution|resolution]] 1.60Å' scene=''> | + | <StructureSection load='4s3j' size='340' side='right'caption='[[4s3j]], [[Resolution|resolution]] 1.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4s3j]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_cereus_10876 Bacillus cereus 10876]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4S3J OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4S3J FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4s3j]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_cereus_ATCC_10876 Bacillus cereus ATCC 10876]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4S3J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4S3J FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4s3k|4s3k]], [[4f55|4f55]], [[4fet|4fet]], [[3cz8|3cz8]]</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=4s3j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4s3j OCA], [https://pdbe.org/4s3j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4s3j RCSB], [https://www.ebi.ac.uk/pdbsum/4s3j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4s3j ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">bcere0002_33520, DJ50_4346 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=526980 Bacillus cereus 10876])</td></tr>
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| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4s3j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4s3j OCA], [http://pdbe.org/4s3j PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4s3j RCSB], [http://www.ebi.ac.uk/pdbsum/4s3j PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4s3j ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus cereus 10876]] | + | [[Category: Bacillus cereus ATCC 10876]] |
| - | [[Category: Chirgadze, D Y]] | + | [[Category: Large Structures]] |
| - | [[Category: Christie, G]] | + | [[Category: Chirgadze DY]] |
| - | [[Category: Ustok, F I]] | + | [[Category: Christie G]] |
| - | [[Category: Hydrolase]] | + | [[Category: Ustok FI]] |
| - | [[Category: N-acetylglucosaminidase]]
| + | |
| - | [[Category: Spore cortex]]
| + | |
| - | [[Category: Tim barrel]]
| + | |
| Structural highlights
Publication Abstract from PubMed
A major event in the germination of Bacillus spores concerns hydrolysis of the cortical peptidoglycan that surrounds the spore protoplast, the integrity of which is essential for maintenance of dormancy. Cortex degradation is initiated in all species of Bacillus spores by the combined activity of two semi-redundant cortex-lytic enzymes, SleB and CwlJ. A third enzyme, SleL, which has N-acetylglucosaminidase activity, cleaves peptidoglycan fragments generated by SleB and CwlJ. Here we present crystal structures of B. cereus and B. megaterium SleL at 1.6 angstroms and 1.7 angstroms, respectively. The structures were determined with a view to identifying the structural basis of differences in catalytic efficiency between the respective enzymes. The catalytic (alpha/beta)8 -barrel cores of both enzymes are highly conserved from a structural perspective, including the spatial distribution of the catalytic residues. Both enzymes are equipped with two N-terminal peptidoglycan-binding LysM domains, which are also structurally highly conserved. However, the topological arrangement of the respective enzymes second LysM domain is markedly different, and this may account for differences in catalytic rates by impacting upon the position of the active sites with respect to their substrates. A chimeric enzyme comprising the B. megaterium SleL catalytic domain plus B. cereus SleL LysM domains displayed enzymatic activity comparable to the native B. cereus protein, exemplifying the importance of the LysM domains to SleL function. Similarly, the reciprocal construct, comprising the B. cereus SleL catalytic domain with B. megaterium SleL LysM domains, showed reduced activity compared with native B. cereus SleL. Proteins 2015. (c) 2015 Wiley Periodicals, Inc.
Structural and functional analysis of SleL, a peptidoglycan lysin involved in germination of Bacillus spores.,Ustok FI, Chirgadze DY, Christie G Proteins. 2015 Jul 18. doi: 10.1002/prot.24861. PMID:26190134[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Ustok FI, Chirgadze DY, Christie G. Structural and functional analysis of SleL, a peptidoglycan lysin involved in germination of Bacillus spores. Proteins. 2015 Jul 18. doi: 10.1002/prot.24861. PMID:26190134 doi:http://dx.doi.org/10.1002/prot.24861
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