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| | ==Crystal structure of Mycobacterial FtsX extracellular domain== | | ==Crystal structure of Mycobacterial FtsX extracellular domain== |
| - | <StructureSection load='4n8n' size='340' side='right' caption='[[4n8n]], [[Resolution|resolution]] 1.87Å' scene=''> | + | <StructureSection load='4n8n' size='340' side='right'caption='[[4n8n]], [[Resolution|resolution]] 1.87Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4n8n]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Myctu Myctu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4N8N OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4N8N FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4n8n]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_H37Rv Mycobacterium tuberculosis H37Rv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4N8N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4N8N FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4n8o|4n8o]]</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=4n8n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4n8n OCA], [https://pdbe.org/4n8n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4n8n RCSB], [https://www.ebi.ac.uk/pdbsum/4n8n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4n8n ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ftsX, MT3185, MTCY164.12c, Rv3101c ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83332 MYCTU])</td></tr>
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| - | <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=4n8n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4n8n OCA], [http://pdbe.org/4n8n PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4n8n RCSB], [http://www.ebi.ac.uk/pdbsum/4n8n PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4n8n ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/FTSX_MYCTU FTSX_MYCTU]] Part of the ABC transporter FtsEX involved in cellular division (By similarity). | + | [https://www.uniprot.org/uniprot/FTSX_MYCTU FTSX_MYCTU] Part of the ABC transporter FtsEX involved in cellular division (By similarity). |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 4n8n" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 4n8n" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Cell division protein 3D structures|Cell division protein 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Myctu]] | + | [[Category: Large Structures]] |
| - | [[Category: Mavrici, D]] | + | [[Category: Mycobacterium tuberculosis H37Rv]] |
| - | [[Category: Cell wall]] | + | [[Category: Mavrici D]] |
| - | [[Category: Membrane protein]]
| + | |
| Structural highlights
Function
FTSX_MYCTU Part of the ABC transporter FtsEX involved in cellular division (By similarity).
Publication Abstract from PubMed
Bacterial growth and cell division are coordinated with hydrolysis of the peptidoglycan (PG) layer of the cell wall, but the mechanisms of regulation of extracellular PG hydrolases are not well understood. Here we report the biochemical, structural, and genetic analysis of the Mycobacterium tuberculosis homolog of the transmembrane PG-hydrolase regulator, FtsX. The purified FtsX extracellular domain binds the PG peptidase Rv2190c/RipC N-terminal segment, causing a conformational change that activates the enzyme. Deletion of ftsEX and ripC caused similar phenotypes in Mycobacterium smegmatis, as expected for genes in a single pathway. The crystal structure of the FtsX extracellular domain reveals an unprecedented fold containing two lobes connected by a flexible hinge. Mutations in the hydrophobic cleft between the lobes reduce RipC binding in vitro and inhibit FtsX function in M. smegmatis. These studies suggest how FtsX recognizes RipC and support a model in which a conformational change in FtsX links the cell division apparatus with PG hydrolysis.
Mycobacterium tuberculosis FtsX extracellular domain activates the peptidoglycan hydrolase, RipC.,Mavrici D, Marakalala MJ, Holton JM, Prigozhin DM, Gee CL, Zhang YJ, Rubin EJ, Alber T Proc Natl Acad Sci U S A. 2014 Jun 3;111(22):8037-42. doi:, 10.1073/pnas.1321812111. Epub 2014 May 19. PMID:24843173[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Mavrici D, Marakalala MJ, Holton JM, Prigozhin DM, Gee CL, Zhang YJ, Rubin EJ, Alber T. Mycobacterium tuberculosis FtsX extracellular domain activates the peptidoglycan hydrolase, RipC. Proc Natl Acad Sci U S A. 2014 Jun 3;111(22):8037-42. doi:, 10.1073/pnas.1321812111. Epub 2014 May 19. PMID:24843173 doi:http://dx.doi.org/10.1073/pnas.1321812111
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