5wam
From Proteopedia
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<StructureSection load='5wam' size='340' side='right' caption='[[5wam]], [[Resolution|resolution]] 2.45Å' scene=''> | <StructureSection load='5wam' size='340' side='right' caption='[[5wam]], [[Resolution|resolution]] 2.45Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5wam]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WAM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5WAM FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5wam]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Neig1 Neig1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WAM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5WAM FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5waq|5waq]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5waq|5waq]]</td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">bamE, NGO_1780 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=242231 NEIG1])</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=5wam FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wam OCA], [http://pdbe.org/5wam PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5wam RCSB], [http://www.ebi.ac.uk/pdbsum/5wam PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5wam ProSAT]</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=5wam FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wam OCA], [http://pdbe.org/5wam PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5wam RCSB], [http://www.ebi.ac.uk/pdbsum/5wam PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5wam ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/Q5F5Y8_NEIG1 Q5F5Y8_NEIG1]] Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane.[HAMAP-Rule:MF_00925] | [[http://www.uniprot.org/uniprot/Q5F5Y8_NEIG1 Q5F5Y8_NEIG1]] Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane.[HAMAP-Rule:MF_00925] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The beta-barrel assembly machinery (BAM) is a conserved multi-component protein complex responsible for the biogenesis of beta-barrel outer membrane proteins (OMPs) in Gram-negative bacteria. Given its role in the production of OMPs for survival and pathogenesis, BAM represents an attractive target for the development of therapeutic interventions including drugs and vaccines against multi-drug resistant bacteria such as Neisseria gonorrhoeae The first structure of BamA, the central component of BAM, was from N. gonorrhoeae, the etiological agent of the sexually transmitted disease gonorrhea. To aid in pharmaceutical targeting of BAM, we expanded our studies to BamD and BamE within BAM of this clinically relevant human pathogen. We found that the presence of BamD, but not BamE, is essential for gonococcal viability. However, BamE, but not BamD, was cell-surface displayed under native conditions, yet in the absence of BamE, BamD indeed becomes surface exposed. Loss of BamE altered cell envelope composition leading to slower growth and increase in both antibiotic susceptibility and formation of membrane vesicles containing greater amounts of vaccine antigens. Both BamD and BamE are expressed in diverse gonococcal isolates, under host-relevant conditions, and throughout different phases of growth. The solved structures of Neisseria BamD and BamE share overall folds with E. coli proteins yet contain differences that may be important for function. Together, these studies highlight that while BAM is conserved across Gram-negative bacteria, structural and functional differences do exist across species, which may be leveraged in the development of species-specific therapeutics in the effort to combat multi-drug resistance. | ||
| + | |||
| + | Structural and functional insights into the role of BamD and BamE within the beta-barrel assembly machinery in Neisseria gonorrhoeae.,Sikora AE, Wierzbicki IH, Zielke RA, Ryner RF, Korotkov KV, Buchanan SK, Noinaj N J Biol Chem. 2017 Dec 11. pii: RA117.000437. doi: 10.1074/jbc.RA117.000437. PMID:29229778<ref>PMID:29229778</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5wam" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Neig1]] | ||
[[Category: Buchanan, S K]] | [[Category: Buchanan, S K]] | ||
[[Category: Korotkov, K V]] | [[Category: Korotkov, K V]] | ||
Revision as of 06:43, 20 December 2017
Structure of BamE from Neisseria gonorrhoeae
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