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| | <StructureSection load='5waq' size='340' side='right'caption='[[5waq]], [[Resolution|resolution]] 2.50Å' scene=''> | | <StructureSection load='5waq' size='340' side='right'caption='[[5waq]], [[Resolution|resolution]] 2.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5waq]] is a 1 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=5WAQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5WAQ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5waq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Neisseria_gonorrhoeae_FA_1090 Neisseria gonorrhoeae FA 1090]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WAQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5WAQ FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5wam|5wam]]</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]] 2.501Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">bamD, NGO_0277 ([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'>[https://proteopedia.org/fgij/fg.htm?mol=5waq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5waq OCA], [https://pdbe.org/5waq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5waq RCSB], [https://www.ebi.ac.uk/pdbsum/5waq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5waq 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=5waq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5waq OCA], [http://pdbe.org/5waq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5waq RCSB], [http://www.ebi.ac.uk/pdbsum/5waq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5waq ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/Q5F9W0_NEIG1 Q5F9W0_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_00922] | + | [https://www.uniprot.org/uniprot/Q5F9W0_NEIG1 Q5F9W0_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_00922] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Neig1]] | + | [[Category: Neisseria gonorrhoeae FA 1090]] |
| - | [[Category: Buchanan, S K]] | + | [[Category: Buchanan SK]] |
| - | [[Category: Korotkov, K V]] | + | [[Category: Korotkov KV]] |
| - | [[Category: Noinaj, N]] | + | [[Category: Noinaj N]] |
| - | [[Category: Bam complex]]
| + | |
| - | [[Category: Beta-barrel assembly machinery]]
| + | |
| - | [[Category: Lipoprotein]]
| + | |
| - | [[Category: Membrane protein]]
| + | |
| - | [[Category: Tetratrico peptide repeat]]
| + | |
| - | [[Category: Tpr domain]]
| + | |
| Structural highlights
Function
Q5F9W0_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_00922]
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Sikora AE, Wierzbicki IH, Zielke RA, Ryner RF, Korotkov KV, Buchanan SK, Noinaj N. Structural and functional insights into the role of BamD and BamE within the beta-barrel assembly machinery in Neisseria gonorrhoeae. J Biol Chem. 2017 Dec 11. pii: RA117.000437. doi: 10.1074/jbc.RA117.000437. PMID:29229778 doi:http://dx.doi.org/10.1074/jbc.RA117.000437
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