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4s3k

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==Crystal structure of the Bacillus megaterium QM B1551 spore cortex-lytic enzyme SleL==
==Crystal structure of the Bacillus megaterium QM B1551 spore cortex-lytic enzyme SleL==
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<StructureSection load='4s3k' size='340' side='right' caption='[[4s3k]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
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<StructureSection load='4s3k' size='340' side='right'caption='[[4s3k]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4s3k]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4S3K OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4S3K FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4s3k]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Priestia_megaterium_QM_B1551 Priestia megaterium QM B1551]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4S3K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4S3K FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4s3j|4s3j]], [[4f55|4f55]], [[4fet|4fet]], [[3cz8|3cz8]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=4s3k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4s3k OCA], [http://pdbe.org/4s3k PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4s3k RCSB], [http://www.ebi.ac.uk/pdbsum/4s3k PDBsum]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4s3k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4s3k OCA], [https://pdbe.org/4s3k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4s3k RCSB], [https://www.ebi.ac.uk/pdbsum/4s3k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4s3k ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/D5DUS2_PRIM1 D5DUS2_PRIM1]
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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.
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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<ref>PMID:26190134</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4s3k" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Chirgadze, D Y]]
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[[Category: Large Structures]]
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[[Category: Christie, G]]
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[[Category: Priestia megaterium QM B1551]]
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[[Category: Ustok, F I]]
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[[Category: Chirgadze DY]]
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[[Category: Hydrolase]]
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[[Category: Christie G]]
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[[Category: N-acetylglucosaminidase]]
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[[Category: Ustok FI]]
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[[Category: Tim barrel]]
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Current revision

Crystal structure of the Bacillus megaterium QM B1551 spore cortex-lytic enzyme SleL

PDB ID 4s3k

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