scholarly journals Crystal structure of the outer membrane protein OmpU fromVibrio choleraeat 2.2 Å resolution

2018 ◽  
Vol 74 (1) ◽  
pp. 21-29 ◽  
Author(s):  
Huanyu Li ◽  
Weijiao Zhang ◽  
Changjiang Dong
Keyword(s):  
Crystal Structure ◽  
Membrane Protein ◽  
Host Cell ◽  
Outer Membrane ◽  
Outer Membrane Protein ◽  
Severe Disease ◽  
Cell Interaction ◽  
Cell Binding ◽  
Important Virulence Factor ◽  
Host Cell Interaction

Vibrio choleraecauses a severe disease that kills thousands of people annually. The outer membrane protein OmpU is the most abundant outer membrane protein inV. cholerae, and has been identified as an important virulence factor that is involved in host-cell interaction and recognition, as well as being critical for the survival of the pathogenicV. choleraein the host body and in harsh environments. The mechanism of these processes is not well understood owing to a lack of the structure ofV. choleraeOmpU. Here, the crystal structure of theV. choleraeOmpU trimer is reported to a resolution of 2.2 Å. The protomer forms a 16-β-stranded barrel with a noncanonical N-terminal coil located in the lumen of the barrel that consists of residues Gly32–Ser42 and is observed to participate in forming the second gate in the pore. By mapping the published functional data onto the OmpU structure, the OmpU structure reinforces the notion that the long extracellular loop L4 with a β-hairpin-like motif may be critical for host-cell binding and invasion, while L3, L4 and L8 are crucially implicated in phage recognition byV. cholerae.

scholarly journals Crystal Structure of the Outer Membrane Protein OpdK from Pseudomonas aeruginosa

Structure ◽  
2008 ◽  
Vol 16 (7) ◽  
pp. 1027-1035 ◽  
Author(s):  
Shyamasri Biswas ◽  
Mohammad M. Mohammad ◽  
Liviu Movileanu ◽  
Bert van den Berg
Keyword(s):  
Crystal Structure ◽  
Pseudomonas Aeruginosa ◽  
Membrane Protein ◽  
Outer Membrane ◽  
Outer Membrane Protein

scholarly journals Evaluation of a Structural Model ofPseudomonas aeruginosa Outer Membrane Protein OprM, an Efflux Component Involved in Intrinsic Antibiotic Resistance

2001 ◽  
Vol 183 (1) ◽  
pp. 367-374 ◽  
Author(s):  
Kendy K. Y. Wong ◽  
Fiona S. L. Brinkman ◽  
Roland S. Benz ◽  
Robert E. W. Hancock
Keyword(s):  
Crystal Structure ◽  
Antibiotic Resistance ◽  
Membrane Protein ◽  
Outer Membrane ◽  
Outer Membrane Protein ◽  
Structural Model ◽  
Sequence Similarity ◽  
Homologous Protein ◽  
Related Family ◽  
Resistance Nodulation Division

ABSTRACT The outer membrane protein OprM of Pseudomonas aeruginosa is involved in intrinsic and mutational multiple-antibiotic resistance as part of two resistance-nodulation-division efflux systems. The crystal structure of TolC, a homologous protein in Escherichia coli, was recently published (V. Koronakis, A. Sharff, E. Koronakis, B. Luisl, and C. Hughes, Nature 405:914–919, 2000), demonstrating a distinctive architecture comprising outer membrane β-barrel and periplasmic helical-barrel structures, which assemble differently from the common β-barrel-only conformation of porins. Based on their sequence similarity, a similar content of α-helical and β-sheet structure determined by circular dichroism spectroscopy, and our observation that OprM, like TolC, reconstitutes channels in planar bilayer membranes, OprM and TolC were considered to be structurally homologous, and a model of OprM was constructed by threading its sequence to the TolC crystal structure. Residues thought to be important for the TolC structure were conserved in space in this OprM model. Analyses of deletion mutants and previously isolated insertion mutants of OprM in the context of this model allowed us to propose roles for different protein domains. Our data indicate that the helical barrel of the protein is critical for both the function and the integrity of the protein, while a C-terminal domain localized around the equatorial plane of this helical barrel is dispensable. Extracellular loops appear to play a lesser role in substrate specificity for this efflux protein compared to classical porins, and there appears to be a correlation between the change in antimicrobial activity for OprM mutants and the pore size. Our model and channel formation studies support the “iris” mechanism of action for TolC and permit us now to form more focused hypotheses about the functional domains of OprM and its related family of efflux proteins.

scholarly journals Crystal Structure of a Major Outer Membrane Protein from Thermus thermophilus HB27

2009 ◽  
Vol 385 (5) ◽  
pp. 1445-1455 ◽  
Author(s):  
Alexander Brosig ◽  
Jutta Nesper ◽  
Winfried Boos ◽  
Wolfram Welte ◽  
Kay Diederichs
Keyword(s):  
Crystal Structure ◽  
Membrane Protein ◽  
Outer Membrane ◽  
Outer Membrane Protein ◽  
Thermus Thermophilus ◽  
Major Outer Membrane Protein

scholarly journals Crystal Structure of Outer Membrane Protein NMB0315 from Neisseria meningitidis

PLoS ONE ◽  
2011 ◽  
Vol 6 (10) ◽  
pp. e26845 ◽  
Author(s):  
Xiangyu Wang ◽  
Xue Yang ◽  
Chunting Yang ◽  
Zhenhua Wu ◽  
Honglin Xu ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Membrane Protein ◽  
Neisseria Meningitidis ◽  
Outer Membrane ◽  
Outer Membrane Protein

scholarly journals Major Surface Protein LipL32 Is Not Required for Either Acute or Chronic Infection with Leptospira interrogans

2008 ◽  
Vol 77 (3) ◽  
pp. 952-958 ◽  
Author(s):  
Gerald L. Murray ◽  
Amporn Srikram ◽  
David E. Hoke ◽  
Elsio A. Wunder ◽  
Rebekah Henry ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Outer Membrane ◽  
Outer Membrane Protein ◽  
Chronic Infection ◽  
Matrix Protein ◽  
Severe Disease ◽  
Extracellular Matrix Protein ◽  
Leptospira Interrogans ◽  
Renal Tubules ◽  
Wild Type

ABSTRACT Leptospira interrogans is responsible for leptospirosis, a zoonosis of worldwide distribution. LipL32 is the major outer membrane protein of pathogenic leptospires, accounting for up to 75% of total outer membrane protein. In recent times LipL32 has become the focus of intense study because of its surface location, dominance in the host immune response, and conservation among pathogenic species. In this study, an lipL32 mutant was constructed in L. interrogans using transposon mutagenesis. The lipL32 mutant had normal morphology and growth rate compared to the wild type and was equally adherent to extracellular matrix. Protein composition of the cell membranes was found to be largely unaffected by the loss of LipL32, with no obvious compensatory increase in other proteins. Microarray studies found no obvious stress response or upregulation of genes that may compensate for the loss of LipL32 but did suggest an association between LipL32 and the synthesis of heme and vitamin B12. When hamsters were inoculated by systemic and mucosal routes, the mutant caused acute severe disease manifestations that were indistinguishable from wild-type L. interrogans infection. In the rat model of chronic infection, the LipL32 mutant colonized the renal tubules as efficiently as the wild-type strain. In conclusion, this study showed that LipL32 does not play a role in either the acute or chronic models of infection. Considering the abundance and conservation of LipL32 among all pathogenic Leptospira spp. and its absence in saprophytic Leptospira, this finding is remarkable. The role of this protein in leptospiral biology and pathogenesis thus remains elusive.

scholarly journals Crystal structure of an antigenic outer-membrane protein from Salmonella Typhi suggests a potential antigenic loop and an efflux mechanism

2015 ◽  
Vol 5 (1) ◽  
Author(s):  
Hong-Hsiang Guan ◽  
Masato Yoshimura ◽  
Phimonphan Chuankhayan ◽  
Chien-Chih Lin ◽  
Nai-Chi Chen ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Membrane Protein ◽  
Outer Membrane ◽  
Outer Membrane Protein ◽  
Salmonella Typhi ◽  
Efflux Mechanism

scholarly journals Crystal structure of an antigenic outer-membrane protein from Salmonella typhi

2017 ◽  
Vol 73 (a2) ◽  
pp. C637-C637
Author(s):  
Chun-Jung Chen ◽  
Hong-Hsiang Guan ◽  
Masato Yoshimura ◽  
Phimonphan Chuankhayan ◽  
Chien-Chih Lin ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Membrane Protein ◽  
Outer Membrane ◽  
Outer Membrane Protein ◽  
Salmonella Typhi
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