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| | ==Crystal structure of Autolysin repeat domains from Staphylococcus epidermidis== | | ==Crystal structure of Autolysin repeat domains from Staphylococcus epidermidis== |
| - | <StructureSection load='4epc' size='340' side='right' caption='[[4epc]], [[Resolution|resolution]] 2.90Å' scene=''> | + | <StructureSection load='4epc' size='340' side='right'caption='[[4epc]], [[Resolution|resolution]] 2.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4epc]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"albococcus_epidermidis"_winslow_and_winslow_1908 "albococcus epidermidis" winslow and winslow 1908]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EPC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4EPC FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4epc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_epidermidis Staphylococcus epidermidis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EPC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EPC FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MLY:N-DIMETHYL-LYSINE'>MLY</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MLY:N-DIMETHYL-LYSINE'>MLY</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">atl, atlE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1282 "Albococcus epidermidis" Winslow and Winslow 1908])</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=4epc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4epc OCA], [https://pdbe.org/4epc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4epc RCSB], [https://www.ebi.ac.uk/pdbsum/4epc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4epc ProSAT]</span></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=4epc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4epc OCA], [http://pdbe.org/4epc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4epc RCSB], [http://www.ebi.ac.uk/pdbsum/4epc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4epc ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [[https://www.uniprot.org/uniprot/ATL_STAEP ATL_STAEP]] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Albococcus epidermidis winslow and winslow 1908]] | + | [[Category: Large Structures]] |
| - | [[Category: N-acetylmuramoyl-L-alanine amidase]] | + | [[Category: Staphylococcus epidermidis]] |
| - | [[Category: Stehle, T]] | + | [[Category: Stehle T]] |
| - | [[Category: Zoll, S]] | + | [[Category: Zoll S]] |
| - | [[Category: Extracellular]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Sh3b fold]]
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| Structural highlights
Function
[ATL_STAEP]
Publication Abstract from PubMed
The bifunctional major autolysin Atl plays a key role in staphylococcal cell separation. Processing of Atl yields catalytically active amidase (AM) and glucosaminidase (GL) domains that are each fused to repeating units. The two repeats of AM (R1 and R2) target the enzyme to the septum, where it cleaves murein between dividing cells. We have determined the crystal structure of R2, which reveals that each repeat folds into two half-open beta-barrel subunits. We furthermore demonstrate that lipoteichoic acid serves as a receptor for the repeats, and that this interaction depends on conserved surfaces in each subunit. Small angle X-ray scattering of the mature amidase reveals the presence of flexible linkers separating the AM, R1 and R2 units. Different levels of flexibility for each linker provide mechanistic insights into the conformational dynamics of the full-length protein and the roles of its components in cell wall association and catalysis. Our analysis supports a model in which the repeats direct the catalytic AM domain to the septum, where it can optimally perform the final step of cell division.
Ligand-binding properties and conformational dynamics of autolysin repeat domains in staphylococcal cell wall recognition.,Zoll S, Schlag M, Shkumatov AV, Rautenberg M, Svergun DI, Gotz F, Stehle T J Bacteriol. 2012 May 18. PMID:22609916[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Zoll S, Schlag M, Shkumatov AV, Rautenberg M, Svergun DI, Gotz F, Stehle T. Ligand-binding properties and conformational dynamics of autolysin repeat domains in staphylococcal cell wall recognition. J Bacteriol. 2012 May 18. PMID:22609916 doi:10.1128/JB.00331-12
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