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Volumn 25, Issue 12, 2016, Pages 2152-2163

The structure of a doripenem-bound OXA-51 class D β-lactamase variant with enhanced carbapenemase activity

Author keywords

antibiotic resistance; carbapenem; crystal structure; lactamase

Indexed keywords

BACTERIAL ENZYME; CARBAPENEMASE; DORIPENEM; INDOLE; ISOLEUCINE; LIGAND; OXA 51 CLASS D BETA LACTAMASE; PENICILLINASE; UNCLASSIFIED DRUG; BETA LACTAMASE; BETA-LACTAMASE OXA-51, ACINETOBACTER BAUMANNII; CARBAPENEM DERIVATIVE;

EID: 84989311551     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.3040     Document Type: Article
Times cited : (23)

References (38)
  • 2
    • 84877928682 scopus 로고    scopus 로고
    • The rise of carbapenem-resistant Acinetobacter baumannii
    • Evans BA, Hamouda A, Amyes SG (2013) The rise of carbapenem-resistant Acinetobacter baumannii. Curr Pharm Des 19:223–238.
    • (2013) Curr Pharm Des , vol.19 , pp. 223-238
    • Evans, B.A.1    Hamouda, A.2    Amyes, S.G.3
  • 4
    • 33746291806 scopus 로고    scopus 로고
    • bla(OXA-51)-type β-lactamase genes are ubiquitous and vary within a strain in Acinetobacter baumannii
    • Merkier AK, Centrón D (2006) bla(OXA-51)-type β-lactamase genes are ubiquitous and vary within a strain in Acinetobacter baumannii. Int J Antimicrob Agents 28:110–113.
    • (2006) Int J Antimicrob Agents , vol.28 , pp. 110-113
    • Merkier, A.K.1    Centrón, D.2
  • 6
    • 84908428517 scopus 로고    scopus 로고
    • Common clinical substitutions enhance the carbapenemase activity of OXA-51-like class D β-lactamases from Acinetobacter spp
    • Mitchell JM, Leonard DA (2014) Common clinical substitutions enhance the carbapenemase activity of OXA-51-like class D β-lactamases from Acinetobacter spp. Antimicrob Agents Chemother 58:7015–7016.
    • (2014) Antimicrob Agents Chemother , vol.58 , pp. 7015-7016
    • Mitchell, J.M.1    Leonard, D.A.2
  • 8
    • 78049311277 scopus 로고    scopus 로고
    • Emergence and distribution of plasmids bearing the blaOXA-51-like gene with an upstream ISAba1 in carbapenem-resistant Acinetobacter baumannii isolates in Taiwan
    • Chen TL, Lee YT, Kuo SC, Hsueh PR, Chang FY, Siu LK, Ko WC, Fung CP (2010) Emergence and distribution of plasmids bearing the blaOXA-51-like gene with an upstream ISAba1 in carbapenem-resistant Acinetobacter baumannii isolates in Taiwan. Antimicrob Agents Chemother 54:4575–4581.
    • (2010) Antimicrob Agents Chemother , vol.54 , pp. 4575-4581
    • Chen, T.L.1    Lee, Y.T.2    Kuo, S.C.3    Hsueh, P.R.4    Chang, F.Y.5    Siu, L.K.6    Ko, W.C.7    Fung, C.P.8
  • 9
    • 84872399119 scopus 로고    scopus 로고
    • Conversion of OXA-66 into OXA-82 in clinical Acinetobacter baumannii isolates and association with altered carbapenem susceptibility
    • Zander E, Chmielarczyk A, Heczko P, Seifert H, Higgins PG (2013) Conversion of OXA-66 into OXA-82 in clinical Acinetobacter baumannii isolates and association with altered carbapenem susceptibility. J Antimicrob Chemother 68:308–311.
    • (2013) J Antimicrob Chemother , vol.68 , pp. 308-311
    • Zander, E.1    Chmielarczyk, A.2    Heczko, P.3    Seifert, H.4    Higgins, P.G.5
  • 10
    • 35848940235 scopus 로고    scopus 로고
    • An OXA-66/OXA-51-like carbapenemase and possibly an efflux pump are associated with resistance to imipenem in Acinetobacter baumannii
    • Hu WS, Yao SM, Fung CP, Hsieh YP, Liu CP, Lin JF (2007) An OXA-66/OXA-51-like carbapenemase and possibly an efflux pump are associated with resistance to imipenem in Acinetobacter baumannii. Antimicrob Agents Chemother 51:3844–3852.
    • (2007) Antimicrob Agents Chemother , vol.51 , pp. 3844-3852
    • Hu, W.S.1    Yao, S.M.2    Fung, C.P.3    Hsieh, Y.P.4    Liu, C.P.5    Lin, J.F.6
  • 12
    • 79951679429 scopus 로고    scopus 로고
    • Structures of the class D carbapenemase OXA-24 from Acinetobacter baumannii in complex with doripenem
    • Schneider KD, Ortega CJ, Renck NA, Bonomo RA, Powers RA, Leonard DA (2011) Structures of the class D carbapenemase OXA-24 from Acinetobacter baumannii in complex with doripenem. J Mol Biol 406:583–594.
    • (2011) J Mol Biol , vol.406 , pp. 583-594
    • Schneider, K.D.1    Ortega, C.J.2    Renck, N.A.3    Bonomo, R.A.4    Powers, R.A.5    Leonard, D.A.6
  • 15
    • 81055145266 scopus 로고    scopus 로고
    • Evolution to carbapenem-hydrolyzing activity in noncarbapenemase class D β-lactamase OXA-10 by rational protein design
    • De Luca F, Benvenuti M, Carboni F, Pozzi C, Rossolini GM, Mangani S, Docquier JD (2011) Evolution to carbapenem-hydrolyzing activity in noncarbapenemase class D β-lactamase OXA-10 by rational protein design. Proc Natl Acad Sci USA 108:18424–18429.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 18424-18429
    • De Luca, F.1    Benvenuti, M.2    Carboni, F.3    Pozzi, C.4    Rossolini, G.M.5    Mangani, S.6    Docquier, J.D.7
  • 17
    • 84884254903 scopus 로고    scopus 로고
    • Structures of the class D Carbapenemases OXA-23 and OXA-146: mechanistic basis of activity against carbapenems, extended-spectrum cephalosporins, and aztreonam
    • Kaitany KC, Klinger NV, June CM, Ramey ME, Bonomo RA, Powers RA, Leonard DA (2013) Structures of the class D Carbapenemases OXA-23 and OXA-146: mechanistic basis of activity against carbapenems, extended-spectrum cephalosporins, and aztreonam. Antimicrob Agents Chemother 57:4848–4855.
    • (2013) Antimicrob Agents Chemother , vol.57 , pp. 4848-4855
    • Kaitany, K.C.1    Klinger, N.V.2    June, C.M.3    Ramey, M.E.4    Bonomo, R.A.5    Powers, R.A.6    Leonard, D.A.7
  • 18
    • 84888615316 scopus 로고    scopus 로고
    • Class D β-lactamases: a reappraisal after five decades
    • Leonard DA, Bonomo RA, Powers RA (2013) Class D β-lactamases: a reappraisal after five decades. Acc Chem Res 46:2407–2415.
    • (2013) Acc Chem Res , vol.46 , pp. 2407-2415
    • Leonard, D.A.1    Bonomo, R.A.2    Powers, R.A.3
  • 19
    • 84992584835 scopus 로고    scopus 로고
    • Clinical variants of the native class D β-lactamase of Acinetobacter baumannii pose an emerging threat through increased hydrolytic activity against carbapenems
    • (in press)
    • Schroder EC, Klamer ZL, Saral A, Sugg KA, June CM, Wymore T, Szarecka A, Leonard DA (in press) Clinical variants of the native class D β-lactamase of Acinetobacter baumannii pose an emerging threat through increased hydrolytic activity against carbapenems. Antimicrob Agents Chemother 60:6155–6164.
    • Antimicrob Agents Chemother , vol.60 , pp. 6155-6164
    • Schroder, E.C.1    Klamer, Z.L.2    Saral, A.3    Sugg, K.A.4    June, C.M.5    Wymore, T.6    Szarecka, A.7    Leonard, D.A.8
  • 20
    • 84921782367 scopus 로고    scopus 로고
    • Evolution of carbapenem-resistant Acinetobacter baumannii revealed through whole-genome sequencing and comparative genomic analysis
    • Li H, Liu F, Zhang Y, Wang X, Zhao C, Chen H, Zhang F, Zhu B, Hu Y, Wang H (2015) Evolution of carbapenem-resistant Acinetobacter baumannii revealed through whole-genome sequencing and comparative genomic analysis. Antimicrob Agents Chemother 59:1168–1176.
    • (2015) Antimicrob Agents Chemother , vol.59 , pp. 1168-1176
    • Li, H.1    Liu, F.2    Zhang, Y.3    Wang, X.4    Zhao, C.5    Chen, H.6    Zhang, F.7    Zhu, B.8    Hu, Y.9    Wang, H.10
  • 21
    • 35148835702 scopus 로고    scopus 로고
    • Eleven novel OXA-51-like enzymes from clinical isolates of Acinetobacter baumannii
    • Evans BA, Brown S, Hamouda A, Findlay J, Amyes SG (2007) Eleven novel OXA-51-like enzymes from clinical isolates of Acinetobacter baumannii. Clin Microbiol Infect 13:1137–1138.
    • (2007) Clin Microbiol Infect , vol.13 , pp. 1137-1138
    • Evans, B.A.1    Brown, S.2    Hamouda, A.3    Findlay, J.4    Amyes, S.G.5
  • 23
    • 38849194030 scopus 로고    scopus 로고
    • OXA-51-like β-lactamases and their association with particular epidemic lineages of Acinetobacter baumannii
    • Evans BA, Hamouda A, Towner KJ, Amyes SG (2008) OXA-51-like β-lactamases and their association with particular epidemic lineages of Acinetobacter baumannii. Clin Microbiol Infect 14:268–275.
    • (2008) Clin Microbiol Infect , vol.14 , pp. 268-275
    • Evans, B.A.1    Hamouda, A.2    Towner, K.J.3    Amyes, S.G.4
  • 24
    • 67650095721 scopus 로고    scopus 로고
    • Mutation of the active site carboxy-lysine (K70) of OXA-1 β-lactamase results in a deacylation-deficient enzyme
    • Schneider KD, Bethel CR, Distler AM, Hujer AM, Bonomo RA, Leonard DA (2009) Mutation of the active site carboxy-lysine (K70) of OXA-1 β-lactamase results in a deacylation-deficient enzyme. Biochemistry 48:6136–6145.
    • (2009) Biochemistry , vol.48 , pp. 6136-6145
    • Schneider, K.D.1    Bethel, C.R.2    Distler, A.M.3    Hujer, A.M.4    Bonomo, R.A.5    Leonard, D.A.6
  • 26
    • 0025856911 scopus 로고
    • Outer membrane permeability of Acinetobacter calcoaceticus and its implication in antibiotic resistance
    • Sato K, Nakae T (1991) Outer membrane permeability of Acinetobacter calcoaceticus and its implication in antibiotic resistance. J Antimicrob Chemother 28:35–45.
    • (1991) J Antimicrob Chemother , vol.28 , pp. 35-45
    • Sato, K.1    Nakae, T.2
  • 27
    • 72449185587 scopus 로고    scopus 로고
    • The 1.4 Å crystal structure of the class D β-lactamase OXA-1 complexed with doripenem
    • Schneider KD, Karpen ME, Bonomo RA, Leonard DA, Powers RA (2009) The 1.4 Å crystal structure of the class D β-lactamase OXA-1 complexed with doripenem. Biochemistry 48:11840–11847.
    • (2009) Biochemistry , vol.48 , pp. 11840-11847
    • Schneider, K.D.1    Karpen, M.E.2    Bonomo, R.A.3    Leonard, D.A.4    Powers, R.A.5
  • 28
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • Gill SC, von Hippel PH (1989) Calculation of protein extinction coefficients from amino acid sequence data. Anal Biochem 182:319–326.
    • (1989) Anal Biochem , vol.182 , pp. 319-326
    • Gill, S.C.1    von Hippel, P.H.2
  • 29
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z, Minor W (1997) Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol 276:307–326.
    • (1997) Methods Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 31
    • 63849246525 scopus 로고    scopus 로고
    • Protein structure prediction on the Web: a case study using the Phyre server
    • Kelley LA, Sternberg MJ (2009) Protein structure prediction on the Web: a case study using the Phyre server. Nat Protoc 4:363–371.
    • (2009) Nat Protoc , vol.4 , pp. 363-371
    • Kelley, L.A.1    Sternberg, M.J.2
  • 32
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov GN, Vagin AA, Dodson EJ (1997) Refinement of macromolecular structures by the maximum-likelihood method. Acta Cryst D53:240–255.
    • (1997) Acta Cryst , vol.D53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 33
    • 0028103275 scopus 로고
    • The CCP4 suite: programs for protein crystallography
    • Collaborative Computational Project #4 (1994) The CCP4 suite: programs for protein crystallography. Acta Cryst D50:760–763.
    • (1994) Acta Cryst , vol.D50 , pp. 760-763
  • 34
    • 13244281317 scopus 로고    scopus 로고
    • Coot: model-building tools for molecular graphics
    • Emsley P, Cowtan K (2004) Coot: model-building tools for molecular graphics. Acta Cryst D60:2126–2132.
    • (2004) Acta Cryst , vol.D60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 37
    • 1942423619 scopus 로고    scopus 로고
    • MMTSB Tool Set: enhanced sampling and multiscale modeling methods for applications in structural biology
    • Feig M, Karanicolas J, Brooks CL (2004) MMTSB Tool Set: enhanced sampling and multiscale modeling methods for applications in structural biology. J Mol Graph Model 22:377–395.
    • (2004) J Mol Graph Model , vol.22 , pp. 377-395
    • Feig, M.1    Karanicolas, J.2    Brooks, C.L.3


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