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| | ==Solution structure of the peptidoglycan binding domain of B. subtilis cell wall lytic enzyme CwlC== | | ==Solution structure of the peptidoglycan binding domain of B. subtilis cell wall lytic enzyme CwlC== |
| - | <StructureSection load='1x60' size='340' side='right'caption='[[1x60]], [[NMR_Ensembles_of_Models | 30 NMR models]]' scene=''> | + | <StructureSection load='1x60' size='340' side='right'caption='[[1x60]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1x60]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"vibrio_subtilis"_ehrenberg_1835 "vibrio subtilis" ehrenberg 1835]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1X60 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1X60 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1x60]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1X60 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1X60 FirstGlance]. <br> |
| - | </td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/N-acetylmuramoyl-L-alanine_amidase N-acetylmuramoyl-L-alanine amidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.28 3.5.1.28] </span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1x60 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1x60 OCA], [https://pdbe.org/1x60 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1x60 RCSB], [https://www.ebi.ac.uk/pdbsum/1x60 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1x60 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=1x60 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1x60 OCA], [https://pdbe.org/1x60 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1x60 RCSB], [https://www.ebi.ac.uk/pdbsum/1x60 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1x60 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/CWLC_BACSU CWLC_BACSU]] Autolysins are involved in some important biological processes such as cell separation, cell-wall turnover, competence for genetic transformation, formation of the flagella - in particular of its basal body - and sporulation. CwlC is able to hydrolyze type A cell walls such as B.subtilis. Its main function is to lyze the mother cell wall peptidoglycan, playing a role during sporulation.<ref>PMID:7601853</ref> <ref>PMID:10945275</ref>
| + | [https://www.uniprot.org/uniprot/CWLC_BACSU CWLC_BACSU] Autolysins are involved in some important biological processes such as cell separation, cell-wall turnover, competence for genetic transformation, formation of the flagella - in particular of its basal body - and sporulation. CwlC is able to hydrolyze type A cell walls such as B.subtilis. Its main function is to lyze the mother cell wall peptidoglycan, playing a role during sporulation.<ref>PMID:7601853</ref> <ref>PMID:10945275</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Vibrio subtilis ehrenberg 1835]] | + | [[Category: Bacillus subtilis]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: N-acetylmuramoyl-L-alanine amidase]]
| + | [[Category: Kato K]] |
| - | [[Category: Kato, K]] | + | [[Category: Kojima C]] |
| - | [[Category: Kojima, C]] | + | [[Category: Mishima M]] |
| - | [[Category: Mishima, M]] | + | [[Category: Sekiguchi J]] |
| - | [[Category: Sekiguchi, J]] | + | [[Category: Shida T]] |
| - | [[Category: Shida, T]] | + | [[Category: Yabuki K]] |
| - | [[Category: Yabuki, K]] | + | |
| - | [[Category: Cell wall lytic amidase]]
| + | |
| - | [[Category: Cwlc]]
| + | |
| - | [[Category: Cwlcr]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Peptidoglycan]]
| + | |
| - | [[Category: Tandem repeat]]
| + | |
| Structural highlights
Function
CWLC_BACSU Autolysins are involved in some important biological processes such as cell separation, cell-wall turnover, competence for genetic transformation, formation of the flagella - in particular of its basal body - and sporulation. CwlC is able to hydrolyze type A cell walls such as B.subtilis. Its main function is to lyze the mother cell wall peptidoglycan, playing a role during sporulation.[1] [2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Bacillus subtilis CwlC is a cell wall lytic N-acetylmuramoyl-l-alanine amidase that plays an important role in mother-cell lysis during sporulation. The enzyme consists of an N-terminal catalytic domain with C-terminal tandem repeats. The repeats [repeat 1 (residues 184-219) and repeat 2 (residues 220-255)] are termed CwlCr. We report on the solution structure of CwlCr as determined by multidimensional NMR, including the use of 36 (h3)J(NC)'-derived hydrogen bond restraints and 64 residual (1)D(NH) dipolar couplings. Two tandem repeats fold into a pseudo-2-fold symmetric single-domain structure consisting of a betaalphabetabetaalphabeta-fold containing numerous contacts between the repeats. Hydrophobic residues important for structural integrity are conserved between the repeats, and are located symmetrically. We also present NMR analysis of the circularly permuted repeat mutant of CwlCr. Secondary structure content from the chemical shifts and hydrogen bonds derived from (h3)J(NC)' show that the mutant folds into a structure similar to that of the wild type, suggesting that the repeats are exchangeable. This implies that conserved hydrophobic residues are crucial for maintaining the folding of the repeats. While monitoring the chemical shift perturbations following the addition of digested soluble peptidoglycan fragments, we identified two peptidoglycan interaction sites of CwlCr at the edges of the protein symmetrically, and they are located approximately 28 A from each other.
Solution structure of the peptidoglycan binding domain of Bacillus subtilis cell wall lytic enzyme CwlC: characterization of the sporulation-related repeats by NMR.,Mishima M, Shida T, Yabuki K, Kato K, Sekiguchi J, Kojima C Biochemistry. 2005 Aug 2;44(30):10153-63. PMID:16042392[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Smith TJ, Foster SJ. Characterization of the involvement of two compensatory autolysins in mother cell lysis during sporulation of Bacillus subtilis 168. J Bacteriol. 1995 Jul;177(13):3855-62. PMID:7601853
- ↑ Shida T, Hattori H, Ise F, Sekiguchi J. Overexpression, purification, and characterization of Bacillus subtilis N-acetylmuramoyl-L-alanine amidase CwlC. Biosci Biotechnol Biochem. 2000 Jul;64(7):1522-5. PMID:10945275
- ↑ Mishima M, Shida T, Yabuki K, Kato K, Sekiguchi J, Kojima C. Solution structure of the peptidoglycan binding domain of Bacillus subtilis cell wall lytic enzyme CwlC: characterization of the sporulation-related repeats by NMR. Biochemistry. 2005 Aug 2;44(30):10153-63. PMID:16042392 doi:10.1021/bi050624n
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