6h5f: Difference between revisions
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<StructureSection load='6h5f' size='340' side='right'caption='[[6h5f]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='6h5f' size='340' side='right'caption='[[6h5f]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6h5f]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6H5F OCA]. For a <b>guided tour on the structure components</b> use [http:// | <table><tr><td colspan='2'>[[6h5f]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Neisseria_meningitidis_nm422 Neisseria meningitidis nm422]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6H5F OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6H5F FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http:// | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">NMB1949 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1095701 Neisseria meningitidis NM422])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6h5f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6h5f OCA], [http://pdbe.org/6h5f PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6h5f RCSB], [http://www.ebi.ac.uk/pdbsum/6h5f PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6h5f ProSAT]</span></td></tr> | |||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Lytic transglycosylases (LT) are enzymes involved in peptidoglycan (PG) remodeling. However, their contribution to cell-wall-modifying complexes and their potential as antimicrobial drug targets remains unclear. Here, we determined a high-resolution structure of the LT, an outer membrane lipoprotein from Neisseria species with a disordered active site helix (alpha helix 30). We show that deletion of the conserved alpha-helix 30 interferes with the integrity of the cell wall, disrupts cell division, cell separation, and impairs the fitness of the human pathogen Neisseria meningitidis during infection. Additionally, deletion of alpha-helix 30 results in hyperacetylated PG, suggesting this LtgA variant affects the function of the PG de-O-acetylase (Ape 1). Our study revealed that Ape 1 requires LtgA for optimal function, demonstrating that LTs can modulate the activity of their protein-binding partner. We show that targeting specific domains in LTs can be lethal, which opens the possibility that LTs are useful drug-targets. | |||
Defective lytic transglycosylase disrupts cell morphogenesis by hindering cell wall de-O-acetylation in Neisseria meningitidis.,Williams AH, Wheeler R, Deghmane AE, Santecchia I, Schaub RE, Hicham S, Moya Nilges M, Malosse C, Chamot-Rooke J, Haouz A, Dillard JP, Robins WP, Taha MK, Gomperts Boneca I Elife. 2020 Feb 5;9. pii: 51247. doi: 10.7554/eLife.51247. PMID:32022687<ref>PMID:32022687</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6h5f" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Neisseria meningitidis nm422]] | |||
[[Category: Williams, A H]] | [[Category: Williams, A H]] | ||
[[Category: Antibiotic resistance]] | [[Category: Antibiotic resistance]] | ||