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| | <StructureSection load='4q2w' size='340' side='right'caption='[[4q2w]], [[Resolution|resolution]] 1.65Å' scene=''> | | <StructureSection load='4q2w' size='340' side='right'caption='[[4q2w]], [[Resolution|resolution]] 1.65Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4q2w]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Strpn Strpn]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Q2W OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4Q2W FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4q2w]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_pneumoniae_TIGR4 Streptococcus pneumoniae TIGR4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Q2W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Q2W FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=4q2w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4q2w OCA], [https://pdbe.org/4q2w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4q2w RCSB], [https://www.ebi.ac.uk/pdbsum/4q2w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4q2w ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">lytB, SP_0965 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=170187 STRPN])</td></tr>
| + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Mannosyl-glycoprotein_endo-beta-N-acetylglucosaminidase Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.96 3.2.1.96] </span></td></tr>
| + | |
| - | <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=4q2w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4q2w OCA], [http://pdbe.org/4q2w PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4q2w RCSB], [http://www.ebi.ac.uk/pdbsum/4q2w PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4q2w ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/LYTB_STRPN LYTB_STRPN]] Plays an important role in cell wall degradation and cell separation (By similarity). | + | [https://www.uniprot.org/uniprot/LYTB_STRPN LYTB_STRPN] Plays an important role in cell wall degradation and cell separation (By similarity). |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase]] | + | [[Category: Streptococcus pneumoniae TIGR4]] |
| - | [[Category: Strpn]]
| + | [[Category: Bai XH]] |
| - | [[Category: Bai, X H]] | + | [[Category: Chen HJ]] |
| - | [[Category: Chen, H J]] | + | [[Category: Chen Y]] |
| - | [[Category: Chen, Y]] | + | [[Category: Cheng W]] |
| - | [[Category: Cheng, W]] | + | [[Category: Jiang YL]] |
| - | [[Category: Jiang, Y L]] | + | [[Category: Li Q]] |
| - | [[Category: Li, Q]] | + | [[Category: Wen Z]] |
| - | [[Category: Wen, Z]] | + | [[Category: Zhang JR]] |
| - | [[Category: Zhang, J R]] | + | [[Category: Zhou CZ]] |
| - | [[Category: Zhou, C Z]] | + | |
| - | [[Category: All-beta module]]
| + | |
| - | [[Category: Gh73]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| Structural highlights
Function
LYTB_STRPN Plays an important role in cell wall degradation and cell separation (By similarity).
Publication Abstract from PubMed
Streptococcus pneumoniae causes a series of devastating infections in humans. Previous studies have shown that the endo-beta-N-acetylglucosaminidase LytB is critical for pneumococcal cell division and nasal colonization, but the biochemical mechanism of LytB action remains unknown. Here we report the 1.65 A crystal structure of the catalytic domain (residues Lys-375-Asp-658) of LytB (termed LytBCAT), excluding the choline binding domain. LytBCAT consists of three structurally independent modules: SH3b, WW, and GH73. These modules form a "T-shaped" pocket that accommodates a putative tetrasaccharide-pentapeptide substrate of peptidoglycan. Structural comparison and simulation revealed that the GH73 module of LytB harbors the active site, including the catalytic residue Glu-564. In vitro assays of hydrolytic activity indicated that LytB prefers the peptidoglycan from the lytB-deficient pneumococci, suggesting the existence of a specific substrate of LytB in the immature peptidoglycan. Combined with in vitro cell-dispersing and in vivo cell separation assays, we demonstrated that all three modules are necessary for the optimal activity of LytB. Further functional analysis showed that the full catalytic activity of LytB is required for pneumococcal adhesion to and invasion into human lung epithelial cells. Structure-based alignment indicated that the unique modular organization of LytB is highly conserved in its orthologs from Streptococcus mitis group and Gemella species. These findings provided structural insights into the pneumococcal cell wall remodeling and novel hints for the rational design of therapeutic agents against pneumococcal growth and thereby the related diseases.
Structure of pneumococcal peptidoglycan hydrolase LytB reveals insights into the bacterial cell wall remodeling and pathogenesis.,Bai XH, Chen HJ, Jiang YL, Wen Z, Huang Y, Cheng W, Li Q, Qi L, Zhang JR, Chen Y, Zhou CZ J Biol Chem. 2014 Aug 22;289(34):23403-16. doi: 10.1074/jbc.M114.579714. Epub, 2014 Jul 7. PMID:25002590[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Bai XH, Chen HJ, Jiang YL, Wen Z, Huang Y, Cheng W, Li Q, Qi L, Zhang JR, Chen Y, Zhou CZ. Structure of pneumococcal peptidoglycan hydrolase LytB reveals insights into the bacterial cell wall remodeling and pathogenesis. J Biol Chem. 2014 Aug 22;289(34):23403-16. doi: 10.1074/jbc.M114.579714. Epub, 2014 Jul 7. PMID:25002590 doi:http://dx.doi.org/10.1074/jbc.M114.579714
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