This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

4y1k

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 13:20, 10 May 2017

PALMITOYLATED OPRM OUTER MEMBRANE FACTOR

Structural highlights

4y1k is a 6 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	3d5k
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[OPRM_PSEAE] The outer membrane component of the MexAB-OprM efflux system that confers multidrug resistance. Also functions as the major efflux pump for n-hexane and p-xylene efflux. Over-expression of the pump increases antibiotic and solvent efflux capacities. Can replace the OprJ outer membrane component of the MexCD-OprJ pump; the antibiotics exported are those exported by the intact MexCD pump, showing that efflux substrate specificity is not conferred by this component. Serves as the outer membrane component for the MexXY efflux system. Implicated in the secretion of the siderophore pyoverdine. OprM is probably involved in the efflux of the siderophore across the outer membrane.^[1] ^[2] ^[3] ^[4] ^[5] The ability to export antibiotics and solvents is dramatically decreased in the presence of the proton conductor carbonyl cyanide m-chlorophenylhydrazone (CCCP), showing that an energized inner membrane is required for efflux. It is thought that the MexB subunit is a proton antiporter.^[6] ^[7] ^[8] ^[9] ^[10]

Publication Abstract from PubMed

Among the different mechanisms used by bacteria to resist antibiotics, active e ffl ux plays a major role. In Gram-negative bacteria, active e ffl ux is carried out by tripartite e ffl ux pumps that form a macromolecular assembly spanning both membranes of the cellular wall. At the outer membrane level, a well-conserved outer membrane factor (OMF) protein acts as an exit duct, but its sequence varies greatly among different species. The OMFs share a similar tri-dimensional structure that includes a beta-barrel pore domain that stabilizes the channel within the membrane. In addition, OMFs are often subjected to different N-terminal post-translational modifications (PTMs), such as an acylation with a lipid. The role of additional N-terminal anchors is all the more intriguing since it is not always required among the OMFs family. Understanding this optional PTM could open new research lines in the field of antibiotics resistance. In Escherichia coli, it has been shown that CusC is modified with a tri-acylated lipid, whereas TolC does not show any modification. In the case of OprM from Pseudomonas aeruginosa, the N-terminal modification remains a matter of debate, therefore, we used several approaches to investigate this issue. As definitive evidence, we present a new X-ray structure at 3.8 A resolution that was solved in a new space group, making it possible to model the N-terminal residue as a palmitoylated cysteine.

New OprM structure highlighting the nature of the N-terminal anchor.,Monlezun L, Phan G, Benabdelhak H, Lascombe MB, Enguene VY, Picard M, Broutin I Front Microbiol. 2015 Jul 1;6:667. doi: 10.3389/fmicb.2015.00667. eCollection, 2015. PMID:26191054^[11]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Poole K, Krebes K, McNally C, Neshat S. Multiple antibiotic resistance in Pseudomonas aeruginosa: evidence for involvement of an efflux operon. J Bacteriol. 1993 Nov;175(22):7363-72. PMID:8226684
↑ Li XZ, Nikaido H, Poole K. Role of mexA-mexB-oprM in antibiotic efflux in Pseudomonas aeruginosa. Antimicrob Agents Chemother. 1995 Sep;39(9):1948-53. PMID:8540696
↑ Srikumar R, Li XZ, Poole K. Inner membrane efflux components are responsible for beta-lactam specificity of multidrug efflux pumps in Pseudomonas aeruginosa. J Bacteriol. 1997 Dec;179(24):7875-81. PMID:9401051
↑ Li XZ, Zhang L, Poole K. Role of the multidrug efflux systems of Pseudomonas aeruginosa in organic solvent tolerance. J Bacteriol. 1998 Jun;180(11):2987-91. PMID:9603892
↑ Masuda N, Sakagawa E, Ohya S, Gotoh N, Tsujimoto H, Nishino T. Contribution of the MexX-MexY-oprM efflux system to intrinsic resistance in Pseudomonas aeruginosa. Antimicrob Agents Chemother. 2000 Sep;44(9):2242-6. PMID:10952562
↑ Poole K, Krebes K, McNally C, Neshat S. Multiple antibiotic resistance in Pseudomonas aeruginosa: evidence for involvement of an efflux operon. J Bacteriol. 1993 Nov;175(22):7363-72. PMID:8226684
↑ Li XZ, Nikaido H, Poole K. Role of mexA-mexB-oprM in antibiotic efflux in Pseudomonas aeruginosa. Antimicrob Agents Chemother. 1995 Sep;39(9):1948-53. PMID:8540696
↑ Srikumar R, Li XZ, Poole K. Inner membrane efflux components are responsible for beta-lactam specificity of multidrug efflux pumps in Pseudomonas aeruginosa. J Bacteriol. 1997 Dec;179(24):7875-81. PMID:9401051
↑ Li XZ, Zhang L, Poole K. Role of the multidrug efflux systems of Pseudomonas aeruginosa in organic solvent tolerance. J Bacteriol. 1998 Jun;180(11):2987-91. PMID:9603892
↑ Masuda N, Sakagawa E, Ohya S, Gotoh N, Tsujimoto H, Nishino T. Contribution of the MexX-MexY-oprM efflux system to intrinsic resistance in Pseudomonas aeruginosa. Antimicrob Agents Chemother. 2000 Sep;44(9):2242-6. PMID:10952562
↑ Monlezun L, Phan G, Benabdelhak H, Lascombe MB, Enguene VY, Picard M, Broutin I. New OprM structure highlighting the nature of the N-terminal anchor. Front Microbiol. 2015 Jul 1;6:667. doi: 10.3389/fmicb.2015.00667. eCollection, 2015. PMID:26191054 doi:http://dx.doi.org/10.3389/fmicb.2015.00667

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4y1k"

@@ Line 1: / Line 1: @@
 ==PALMITOYLATED OPRM OUTER MEMBRANE FACTOR==
 <StructureSection load='4y1k' size='340' side='right' caption='[[4y1k]], [[Resolution|resolution]] 3.80&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PLM:PALMITIC+ACID'>PLM</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3d5k|3d5k]]</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=4y1k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4y1k OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4y1k RCSB], [http://www.ebi.ac.uk/pdbsum/4y1k PDBsum]</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=4y1k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4y1k OCA], [http://pdbe.org/4y1k PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4y1k RCSB], [http://www.ebi.ac.uk/pdbsum/4y1k PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4y1k ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 17: / Line 18: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4y1k" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Porin|Porin]]
 == References ==
 <references/>

4y1k

From Proteopedia

Revision as of 13:20, 10 May 2017

PALMITOYLATED OPRM OUTER MEMBRANE FACTOR

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox