|
|
| Line 3: |
Line 3: |
| | <StructureSection load='4x36' size='340' side='right'caption='[[4x36]], [[Resolution|resolution]] 2.10Å' scene=''> | | <StructureSection load='4x36' size='340' side='right'caption='[[4x36]], [[Resolution|resolution]] 2.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4x36]] 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=4X36 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4X36 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4x36]] 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=4X36 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4X36 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CHT:CHOLINE+ION'>CHT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CHT:CHOLINE+ION'>CHT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=4x36 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4x36 OCA], [https://pdbe.org/4x36 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4x36 RCSB], [https://www.ebi.ac.uk/pdbsum/4x36 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4x36 ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">lytA, SP_1937 ([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/N-acetylmuramoyl-L-alanine_amidase N-acetylmuramoyl-L-alanine amidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.28 3.5.1.28] </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=4x36 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4x36 OCA], [http://pdbe.org/4x36 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4x36 RCSB], [http://www.ebi.ac.uk/pdbsum/4x36 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4x36 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/ALYS_STRPN ALYS_STRPN]] Autolysins are involved in some important biological processes such as cell separation, cell-wall turnover, competence for genetic transformation, formation of the flagella and sporulation. Autolysin strictly depends on the presence of choline-containing cell walls for activity. | + | [https://www.uniprot.org/uniprot/ALYS_STRPN ALYS_STRPN] Autolysins are involved in some important biological processes such as cell separation, cell-wall turnover, competence for genetic transformation, formation of the flagella and sporulation. Autolysin strictly depends on the presence of choline-containing cell walls for activity. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 26: |
Line 23: |
| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: N-acetylmuramoyl-L-alanine amidase]] | + | [[Category: Streptococcus pneumoniae TIGR4]] |
| - | [[Category: Strpn]]
| + | [[Category: Chen YX]] |
| - | [[Category: Chen, Y X]] | + | [[Category: Cheng W]] |
| - | [[Category: Cheng, W]] | + | [[Category: Li Q]] |
| - | [[Category: Li, Q]] | + | [[Category: Zhou CZ]] |
| - | [[Category: Zhou, C Z]] | + | |
| - | [[Category: Amidase]]
| + | |
| - | [[Category: Autolysin]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| Structural highlights
Function
ALYS_STRPN Autolysins are involved in some important biological processes such as cell separation, cell-wall turnover, competence for genetic transformation, formation of the flagella and sporulation. Autolysin strictly depends on the presence of choline-containing cell walls for activity.
Publication Abstract from PubMed
LytA is responsible for the autolysis of many Streptococcus species, including pathogens such as S. pneumoniae, S. pseudopneumoniae and S. mitis. However, how this major autolysin achieves full activity remains unknown. Here, the full-length structure of the S. pneumoniae LytA dimer is reported at 2.1 A resolution. Each subunit has an N-terminal amidase domain and a C-terminal choline-binding domain consisting of six choline-binding repeats, which form five canonical and one single-layered choline-binding sites. Site-directed mutageneses combined with enzymatic activity assays indicate that dimerization and binding to choline are two independent requirements for the autolytic activity of LytA in vivo. Altogether, it is suggested that dimerization and full occupancy of all choline-binding sites through binding to choline-containing TA chains enable LytA to adopt a fully active conformation which allows the amidase domain to cleave two lactyl-amide bonds located about 103 A apart on the peptidoglycan.
Full-length structure of the major autolysin LytA.,Li Q, Cheng W, Morlot C, Bai XH, Jiang YL, Wang W, Roper DI, Vernet T, Dong YH, Chen Y, Zhou CZ Acta Crystallogr D Biol Crystallogr. 2015 Jun;71(Pt 6):1373-81. doi:, 10.1107/S1399004715007403. Epub 2015 May 23. PMID:26057677[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Li Q, Cheng W, Morlot C, Bai XH, Jiang YL, Wang W, Roper DI, Vernet T, Dong YH, Chen Y, Zhou CZ. Full-length structure of the major autolysin LytA. Acta Crystallogr D Biol Crystallogr. 2015 Jun;71(Pt 6):1373-81. doi:, 10.1107/S1399004715007403. Epub 2015 May 23. PMID:26057677 doi:http://dx.doi.org/10.1107/S1399004715007403
|
