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| | <StructureSection load='4bh5' size='340' side='right'caption='[[4bh5]], [[Resolution|resolution]] 1.57Å' scene=''> | | <StructureSection load='4bh5' size='340' side='right'caption='[[4bh5]], [[Resolution|resolution]] 1.57Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4bh5]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BH5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BH5 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4bh5]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BH5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BH5 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.57Å</td></tr> |
| | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</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=4bh5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bh5 OCA], [https://pdbe.org/4bh5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bh5 RCSB], [https://www.ebi.ac.uk/pdbsum/4bh5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bh5 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=4bh5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bh5 OCA], [https://pdbe.org/4bh5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bh5 RCSB], [https://www.ebi.ac.uk/pdbsum/4bh5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bh5 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/ENVC_ECOLI ENVC_ECOLI]] Activator of the cell wall hydrolases AmiA and AmiB. Required for septal murein cleavage and daughter cell separation during cell division. In vitro, exhibits weak endoproteolytic activity on beta-casein.<ref>PMID:11976287</ref> <ref>PMID:15165230</ref> <ref>PMID:19525345</ref> <ref>PMID:20300061</ref>
| + | [https://www.uniprot.org/uniprot/ENVC_ECOLI ENVC_ECOLI] Activator of the cell wall hydrolases AmiA and AmiB. Required for septal murein cleavage and daughter cell separation during cell division. In vitro, exhibits weak endoproteolytic activity on beta-casein.<ref>PMID:11976287</ref> <ref>PMID:15165230</ref> <ref>PMID:19525345</ref> <ref>PMID:20300061</ref> |
| | <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: Ecoli]] | + | [[Category: Escherichia coli K-12]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Bernhardt, T G]] | + | [[Category: Bernhardt TG]] |
| - | [[Category: Morlot, C]] | + | [[Category: Morlot C]] |
| - | [[Category: Peters, N T]] | + | [[Category: Peters NT]] |
| - | [[Category: Uehara, T]] | + | [[Category: Uehara T]] |
| - | [[Category: Vernet, T]] | + | [[Category: Vernet T]] |
| - | [[Category: Yang, D C]] | + | [[Category: Yang DC]] |
| - | [[Category: Amidase activator]]
| + | |
| - | [[Category: Autolysin]]
| + | |
| - | [[Category: Cell cycle]]
| + | |
| - | [[Category: Cytokinesis]]
| + | |
| - | [[Category: Morphogenesis]]
| + | |
| - | [[Category: Peptidoglycan]]
| + | |
| - | [[Category: Sacculus]]
| + | |
| Structural highlights
Function
ENVC_ECOLI Activator of the cell wall hydrolases AmiA and AmiB. Required for septal murein cleavage and daughter cell separation during cell division. In vitro, exhibits weak endoproteolytic activity on beta-casein.[1] [2] [3] [4]
Publication Abstract from PubMed
Proteins with LytM (Peptidase_M23) domains are broadly distributed in bacteria and have been implicated in a variety of important processes, including cell division and cell-shape determination. Most LytM-like proteins that have been structurally and/or biochemically characterized are metallo-endopeptidases that cleave crosslinks in the peptidoglycan (PG) cell wall matrix. Notable exceptions are the Escherichia coli cell division proteins EnvC and NlpD. These LytM factors are not hydrolases themselves, but instead serve as activators that stimulate PG cleavage by target enzymes called amidases to promote cell separation. Here we report the structure of the LytM domain from EnvC, the first structure of a LytM factor implicated in the regulation of PG hydrolysis. As expected, the fold is highly similar to that of other LytM proteins. However, consistent with its role as a regulator, the active site region is degenerate and lacks a catalytic metal ion. Importantly, genetic analysis indicates that residues in and around this degenerate active site are critical for amidase activation in vivo and in vitro. Thus, in the regulatory LytM factors, the apparent substrate binding pocket conserved in active metallo-endopeptidases has been adapted to control PG hydrolysis by another set of enzymes.
Structure-function analysis of the LytM domain of EnvC, an activator of cell wall remodeling at the Escherichia coli division site.,Peters NT, Morlot C, Yang DC, Uehara T, Vernet T, Bernhardt TG Mol Microbiol. 2013 Jun 25. doi: 10.1111/mmi.12304. PMID:23796240[5]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Ichimura T, Yamazoe M, Maeda M, Wada C, Hiraga S. Proteolytic activity of YibP protein in Escherichia coli. J Bacteriol. 2002 May;184(10):2595-602. PMID:11976287
- ↑ Bernhardt TG, de Boer PA. Screening for synthetic lethal mutants in Escherichia coli and identification of EnvC (YibP) as a periplasmic septal ring factor with murein hydrolase activity. Mol Microbiol. 2004 Jun;52(5):1255-69. PMID:15165230 doi:10.1111/j.1365-2958.2004.04063.x
- ↑ Uehara T, Dinh T, Bernhardt TG. LytM-domain factors are required for daughter cell separation and rapid ampicillin-induced lysis in Escherichia coli. J Bacteriol. 2009 Aug;191(16):5094-107. doi: 10.1128/JB.00505-09. Epub 2009 Jun, 12. PMID:19525345 doi:10.1128/JB.00505-09
- ↑ Uehara T, Parzych KR, Dinh T, Bernhardt TG. Daughter cell separation is controlled by cytokinetic ring-activated cell wall hydrolysis. EMBO J. 2010 Apr 21;29(8):1412-22. doi: 10.1038/emboj.2010.36. Epub 2010 Mar 18. PMID:20300061 doi:10.1038/emboj.2010.36
- ↑ Peters NT, Morlot C, Yang DC, Uehara T, Vernet T, Bernhardt TG. Structure-function analysis of the LytM domain of EnvC, an activator of cell wall remodeling at the Escherichia coli division site. Mol Microbiol. 2013 Jun 25. doi: 10.1111/mmi.12304. PMID:23796240 doi:10.1111/mmi.12304
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