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Proteome and differential expression analysis of membrane and cytosolic proteins from Mycobacterium avium subsp. paratuberculosis strains K-10 and 187
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Structure of the fibre-forming protein pilin at 2.6 A resolution
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Meningococcal pilin: a glycoprotein substituted with digalactosyl 2,4-diacetamido-2,4,6-trideoxyhexose
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Neisseria gonorrhoeae type IV pili undergo multisite, hierarchical modifications with phosphoethanolamine and phosphocholine requiring an enzyme structurally related to lipopolysaccharide phosphoethanolamine transferases
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The top-down MS approach, in which PTMs can be detected directly from intact proteins, was applied in this paper and it can alleviate the problems of a bottom-up approach in which proteolytically derived peptides were examined by MS/MS.
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Aas F.E., Egge-Jacobsen W., Winther-Larsen H.C., Lovold C., Hitchen P.G., Dell A., and Koomey M. Neisseria gonorrhoeae type IV pili undergo multisite, hierarchical modifications with phosphoethanolamine and phosphocholine requiring an enzyme structurally related to lipopolysaccharide phosphoethanolamine transferases. J Biol Chem 281 (2006) 27712-27723. The top-down MS approach, in which PTMs can be detected directly from intact proteins, was applied in this paper and it can alleviate the problems of a bottom-up approach in which proteolytically derived peptides were examined by MS/MS.
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J Biol Chem
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Functional analysis of the Campylobacter jejuni N-linked protein glycosylation pathway
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Linton D., Dorrell N., Hitchen P.G., Amber S., Karlyshev A.V., Morris H.R., Dell A., Valvano M.A., Aebi M., and Wren B.W. Functional analysis of the Campylobacter jejuni N-linked protein glycosylation pathway. Mol Microbiol 55 (2005) 1695-1703
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49
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Proteomic identification of M. tuberculosis protein kinase substrates: PknB recruits GarA, a FHA domain-containing protein, through activation loop-mediated interactions
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The authors report the identification of GarA, as a putative physiological substrate of an essential protein kinase, PknB, in M. tuberculosis using a global proteomic approach that combined 2-DE, autoradiography, and MS identification. They further investigated protein kinase-substrate interactions by MS, enzymological, and binding studies of wild-type and mutant proteins.
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Villarino A., Duran R., Wehenkel A., Fernandez P., England P., Brodin P., Cole S.T., Zimny-Arndt U., Jungblut P.R., Cervenansky C., et al. Proteomic identification of M. tuberculosis protein kinase substrates: PknB recruits GarA, a FHA domain-containing protein, through activation loop-mediated interactions. J Mol Biol 350 (2005) 953-963. The authors report the identification of GarA, as a putative physiological substrate of an essential protein kinase, PknB, in M. tuberculosis using a global proteomic approach that combined 2-DE, autoradiography, and MS identification. They further investigated protein kinase-substrate interactions by MS, enzymological, and binding studies of wild-type and mutant proteins.
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J Mol Biol
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Villarino, A.1
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Jungblut, P.R.9
Cervenansky, C.10
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50
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34548139422
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Structure and function of an essential component of the outer membrane protein assembly machine
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This is an excellent work solving the crystal structure of a fragment of the Omp85-family member YaeT from E. coli. The fragment encompasses four complete polypeptide transport-associated (POTRA) domains and a short segment of the fifth one at the carboxyl terminus.
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Kim S., Malinverni J.C., Sliz P., Silhavy T.J., Harrison S.C., and Kahne D. Structure and function of an essential component of the outer membrane protein assembly machine. Science 317 (2007) 961-964. This is an excellent work solving the crystal structure of a fragment of the Omp85-family member YaeT from E. coli. The fragment encompasses four complete polypeptide transport-associated (POTRA) domains and a short segment of the fifth one at the carboxyl terminus.
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Science
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Kim, S.1
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Kahne, D.6
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51
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34548128883
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Structure of the membrane protein FhaC: a member of the Omp85-TpsB transporter superfamily
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This is an excellent study solving the crystal structure of FhaC, a member of the Omp85 superfamily involved in the secretion of filamentous hemagglutinin (FHA) in Bordetella pertussis. The structure shows a 16-stranded β barrel that is occluded by an N-terminal α helix and an extracellular loop and two periplasmic POTRA domains structurally resembling those of YaeT.
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Clantin B., Delattre A.S., Rucktooa P., Saint N., Meli A.C., Locht C., Jacob-Dubuisson F., and Villeret V. Structure of the membrane protein FhaC: a member of the Omp85-TpsB transporter superfamily. Science 317 (2007) 957-961. This is an excellent study solving the crystal structure of FhaC, a member of the Omp85 superfamily involved in the secretion of filamentous hemagglutinin (FHA) in Bordetella pertussis. The structure shows a 16-stranded β barrel that is occluded by an N-terminal α helix and an extracellular loop and two periplasmic POTRA domains structurally resembling those of YaeT.
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Science
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Clantin, B.1
Delattre, A.S.2
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Locht, C.6
Jacob-Dubuisson, F.7
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52
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Structural basis for the specific inhibition of protein kinase G, a virulence factor of Mycobacterium tuberculosis
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Scherr N., Honnappa S., Kunz G., Mueller P., Jayachandran R., Winkler F., Pieters J., and Steinmetz M.O. Structural basis for the specific inhibition of protein kinase G, a virulence factor of Mycobacterium tuberculosis. Proc Natl Acad Sci U S A 104 (2007) 12151-12156
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Structural basis for evasion of IgA immunity by Staphylococcus aureus revealed in the complex of SSL7 with Fc of human IgA1
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The authors report the X-ray crystal structure of protein kinase G (PknG) in complex with the inhibitor, AX20017. The structure of PknG consists of a central kinase domain that is flanked by N- and C-terminal rubredoxin and tetratrico-peptide repeat domains, respectively, and the rubredoxin domain is essential for the PknG activity.
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Ramsland P.A., Willoughby N., Trist H.M., Farrugia W., Hogarth P.M., Fraser J.D., and Wines B.D. Structural basis for evasion of IgA immunity by Staphylococcus aureus revealed in the complex of SSL7 with Fc of human IgA1. Proc Natl Acad Sci U S A 104 (2007) 15051-15056. The authors report the X-ray crystal structure of protein kinase G (PknG) in complex with the inhibitor, AX20017. The structure of PknG consists of a central kinase domain that is flanked by N- and C-terminal rubredoxin and tetratrico-peptide repeat domains, respectively, and the rubredoxin domain is essential for the PknG activity.
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Proc Natl Acad Sci U S A
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Ramsland, P.A.1
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Fraser, J.D.6
Wines, B.D.7
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54
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Solution structure of monomeric BsaL, the type III secretion needle protein of Burkholderia pseudomallei
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Zhang L., Wang Y., Picking W.L., Picking W.D., and De Guzman R.N. Solution structure of monomeric BsaL, the type III secretion needle protein of Burkholderia pseudomallei. J Mol Biol 359 (2006) 322-330
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J Mol Biol
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Zhang, L.1
Wang, Y.2
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De Guzman, R.N.5
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55
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33747872707
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Type IV pilus structure by cryo-electron microscopy and crystallography: implications for pilus assembly and functions
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The Type IV pilus (T4P) structure of N. gonorrhoeae was determined by quantitative fitting of a 2.3 Å full-length pilin crystal structure into a 12.5 Å resolution native T4P solved by cryo-electron microscopy.
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Craig L., Volkmann N., Arvai A.S., Pique M.E., Yeager M., Egelman E.H., and Tainer J.A. Type IV pilus structure by cryo-electron microscopy and crystallography: implications for pilus assembly and functions. Mol Cell 23 (2006) 651-662. The Type IV pilus (T4P) structure of N. gonorrhoeae was determined by quantitative fitting of a 2.3 Å full-length pilin crystal structure into a 12.5 Å resolution native T4P solved by cryo-electron microscopy.
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(2006)
Mol Cell
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Craig, L.1
Volkmann, N.2
Arvai, A.S.3
Pique, M.E.4
Yeager, M.5
Egelman, E.H.6
Tainer, J.A.7
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