메뉴 건너뛰기




Volumn 77, Issue 3, 2009, Pages 741-746

Crystal structure of the manganese transport regulatory protein from Escherichia coli

Author keywords

Escherichia coli; JW0801; Metal homeostasis; MntR; Transcriptional regulator; X ray structure

Indexed keywords

ESCHERICHIA COLI PROTEIN; MANGANESE TRANSPORT REGULATOR PROTEIN; METAL ION; REGULATOR PROTEIN; UNCLASSIFIED DRUG;

EID: 70349310256     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.22541     Document Type: Article
Times cited : (9)

References (35)
  • 1
    • 0027183546 scopus 로고
    • Transition metals in control of gene expression
    • O'halloran TV. Transition metals in control of gene expression. Science 1993;261:715-725.
    • (1993) Science , vol.261 , pp. 715-725
    • O'Halloran, T.V.1
  • 2
    • 27644580799 scopus 로고    scopus 로고
    • Understanding how cells allocate metals using metal sensors and metallochaperones
    • Tottey S, Harvie DR, Robinson NJ. Understanding how cells allocate metals using metal sensors and metallochaperones. Acc Chem Res 2005;38:775-783.
    • (2005) Acc Chem Res , vol.38 , pp. 775-783
    • Tottey, S.1    Harvie, D.R.2    Robinson, N.J.3
  • 3
    • 0013098131 scopus 로고    scopus 로고
    • Outten FW, Outten CE, O'halloran TV. Storz G, Hengge-Aronis R, editors. Washington: ASM
    • Outten FW, Outten CE, O'halloran TV. Storz G, Hengge-Aronis R, editors. Bacterial stress responses. Washington: ASM; 2000. pp 145-157.
    • (2000) Bacterial Stress Responses , pp. 145-157
  • 4
    • 0033624818 scopus 로고    scopus 로고
    • Manganese homestasis in Bacillus subtilis is regulated by MntR, a bifunctional regulator related to the diphtheria toxin repressor family of proteins
    • DOI 10.1046/j.1365-2958.2000.01811.x
    • Que Q, Helmann JD. Manganese homeostasis in Bacillus subtilis is regulated by MntR, a bifunctional regulator related to the diphtheria toxin repressor family of proteins. Mol Microbiol 2000;35:1454-1468. (Pubitemid 30175521)
    • (2000) Molecular Microbiology , vol.35 , Issue.6 , pp. 1454-1468
    • Que, Q.1    Helmann, J.D.2
  • 5
    • 0034902162 scopus 로고    scopus 로고
    • 2+ transporter in Escherichia coli
    • 2+ transporter in Escherichia coli. J Bacteriol 2001;183:4806-4813.
    • (2001) J Bacteriol , vol.183 , pp. 4806-4813
    • Patzer, S.I.1    Hantke, K.2
  • 6
    • 0038349048 scopus 로고    scopus 로고
    • Origins of metal ion selectivity in the DtxR/MntR family of metalloregulators
    • DOI 10.1046/j.1365-2958.2003.03445.x
    • Guedon E, Helmann JD. Origins of metal ion selectivity in the DtxR/MntR family of metalloregulators. Mol Microbiol 2003;48:495-506. (Pubitemid 36819084)
    • (2003) Molecular Microbiology , vol.48 , Issue.2 , pp. 495-506
    • Guedon, E.1    Helmann, J.D.2
  • 7
    • 0242318378 scopus 로고    scopus 로고
    • DNA-binding and oligomerization studies of the manganese(II) metalloregulatory protein MntR from Bacillus subtilis
    • Lieser SA, Davis TC, Helmann JD, Cohen SM. DNA-binding and oligomerization studies of the manganese(II) metalloregulatory protein MntR from Bacillus subtilis. Biochemistry 2003;42:12634-12642.
    • (2003) Biochemistry , vol.42 , pp. 12634-12642
    • Lieser, S.A.1    Davis, T.C.2    Helmann, J.D.3    Cohen, S.M.4
  • 9
    • 0015848173 scopus 로고
    • Superoxide dismutase:Organelle specificity
    • Weisiger RA, Fridovich I. Superoxide dismutase:Organelle specificity. J Biol Chem 1973;248:3582-3592.
    • (1973) J Biol Chem , vol.248 , pp. 3582-3592
    • Weisiger, R.A.1    Fridovich, I.2
  • 10
    • 0038240674 scopus 로고    scopus 로고
    • Emerging themes in manganese transport, biochemistry and pathogenesis in bacteria
    • Kehres DG, Maguire ME. Emerging themes in manganese transport, biochemistry and pathogenesis in bacteria. FEMS Microbiol Rev 2003;27:263-290.
    • (2003) FEMS Microbiol Rev , vol.27 , pp. 263-290
    • Kehres, D.G.1    Maguire, M.E.2
  • 12
    • 26944486892 scopus 로고    scopus 로고
    • The solute-binding component of a putative Mn(II) ABC transporter (MntA) is a novel Bacillus anthracis virulence determinant
    • DOI 10.1111/j.1365-2958.2005.04848.x
    • Gat O, Mendelson I, Chitlaru T, Ariel N, Altboum Z, Levy H, Weiss S, Grosfeld H, Cohen S, Shafferman A. The solute-binding component of a putative Mn(II) ABC transporter (MntA) is a novel Bacillus anthracis virulence determinant. Mol Microbiol 2005;58:533-551. (Pubitemid 41476167)
    • (2005) Molecular Microbiology , vol.58 , Issue.2 , pp. 533-551
    • Gat, O.1    Mendelson, I.2    Chitlaru, T.3    Ariel, N.4    Altboum, Z.5    Levy, H.6    Weiss, S.7    Grosfeld, H.8    Cohen, S.9    Shafferman, A.10
  • 13
    • 0025300518 scopus 로고
    • Molecular cloning and DNA sequence analysis of a diphtheria tox iron-dependent regulatory element (dtxR) from Corynebacterium diphtheriae
    • DOI 10.1073/pnas.87.15.5968
    • Boyd J, Oza MN, Murphy JR. Molecular cloning and DNA sequence analysis of a diphtheria tox iron-dependent regulatory element (dtxR) from Corynebacterium diphtheriae. Proc Natl Acad Sci USA 1990;87:5968-5972. (Pubitemid 20240411)
    • (1990) Proceedings of the National Academy of Sciences of the United States of America , vol.87 , Issue.15 , pp. 5968-5972
    • Boyd, J.1    Oza, M.N.2    Murphy, J.R.3
  • 14
    • 0035937172 scopus 로고    scopus 로고
    • Crystal Structure of the Iron-dependent Regulator from Mycobacterium tuberculosis at 2.0-Å Resolution Reveals the Src Homology Domain 3-like Fold and Metal Binding Function of the Third Domain
    • DOI 10.1074/jbc.M007531200
    • Feese MD, Ingason BP, Goranson-Siekierke J, Holmes RK, Hol WGJ. Crystal structure of the iron-dependent regulator from Mycobacterium tuberculosis at 2.0Å resolution reveals the Src homology domain 3-like fold and metal binding function of the third domain. J Biol Chem 2001;276:5959-5966. (Pubitemid 37385753)
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.8 , pp. 5959-5966
    • Feese, M.D.1    Ingason, B.P.2    Goranson-Siekierke, J.3    Holmes, R.K.4    Hol, W.G.J.5
  • 15
    • 0042624650 scopus 로고    scopus 로고
    • Structure of the manganese-bound manganese transport regulator of Bacillus subtilis
    • DOI 10.1038/nsb951
    • Glasfeld A, Guedon E, Helmann JD, Brennan RG. Structure of the manganese-bound manganese transport regulator of Bacillus subtilis. Nat Struct Biol 2003;10:652-657. (Pubitemid 36944719)
    • (2003) Nature Structural Biology , vol.10 , Issue.8 , pp. 652-657
    • Glasfeld, A.1    Guedon, E.2    Helmann, J.D.3    Brennan, R.G.4
  • 16
    • 14644437027 scopus 로고    scopus 로고
    • Metalinduced structural organization and stabilization of the metalloregulatory protein MntR
    • Golynskiy MV, Davis TC, Helmann JD, Cohen SM. Metalinduced structural organization and stabilization of the metalloregulatory protein MntR. Biochemistry 2005;44:3380-3389.
    • (2005) Biochemistry , vol.44 , pp. 3380-3389
    • Golynskiy, M.V.1    Davis, T.C.2    Helmann, J.D.3    Cohen, S.M.4
  • 17
    • 33645244097 scopus 로고    scopus 로고
    • Structural basis for the metal-selective activation of the manganese transport regulator of Bacillus subtilis
    • Kliegman JI, Griner SL, Helmann JD, Brennan RG, Glasfeld A. Structural basis for the metal-selective activation of the manganese transport regulator of Bacillus subtilis. Biochemistry 2006;45:3493-3505.
    • (2006) Biochemistry , vol.45 , pp. 3493-3505
    • Kliegman, J.I.1    Griner, S.L.2    Helmann, J.D.3    Brennan, R.G.4    Glasfeld, A.5
  • 18
    • 33846026683 scopus 로고    scopus 로고
    • The Conformations of the Manganese Transport Regulator of Bacillus subtilis in its Metal-free State
    • DOI 10.1016/j.jmb.2006.10.080, PII S0022283606015051
    • Dewitt MA, Kliegman JI, Helmann JD, Brennan RG, Farrens DL, Glasfeld A. The conformations of the manganese transport regulator of Bacillus subtilis in its metal-free state. J Mol Biol 2007;365:1257-1265. (Pubitemid 46048834)
    • (2007) Journal of Molecular Biology , vol.365 , Issue.5 , pp. 1257-1265
    • Dewitt, M.A.1    Kliegman, J.I.2    Helmann, J.D.3    Brennan, R.G.4    Farrens, D.L.5    Glasfeld, A.6
  • 19
    • 0028826149 scopus 로고
    • Structures of the apo- And the metal ion-activated forms of the diphtheria tox repressor from Corynebacterium diphtheriae
    • Schiering N, Tao X, Zeng H, Murphy JR, Petsko GA, Ringe D. Structures of the apo- and the metal ion-activated forms of the diphtheria tox repressor from Corynebacterium diphtheriae. Proc Natl Acad Sci USA 1995;1995:9843-9850.
    • (1995) Proc Natl Acad Sci USA , vol.1995 , pp. 9843-9850
    • Schiering, N.1    Tao, X.2    Zeng, H.3    Murphy, J.R.4    Petsko, G.A.5    Ringe, D.6
  • 20
    • 0001590980 scopus 로고    scopus 로고
    • Crystal structure of the iron-dependent regulator (IdeR) from Mycobacterium tuberculosis shows both metal binding sites fully occupied
    • DOI 10.1006/jmbi.1998.2339
    • Pohl E, Holmes RK, Hol WGJ. Crystal structure of the iron-dependent regulator (IdeR) from Mycobacerium tuberculosis shows both metal binding sites fully occupied. J Mol Biol 1999;285:1145-1156. (Pubitemid 29054322)
    • (1999) Journal of Molecular Biology , vol.285 , Issue.3 , pp. 1145-1156
    • Pohl, E.1    Holmes, R.K.2    Hol, W.G.J.3
  • 21
    • 0000868851 scopus 로고    scopus 로고
    • Crystal structure of a cobalt-activated diphtheria toxin repressor-DNA complex reveals a metal-binding SH3-like domain
    • DOI 10.1006/jmbi.1999.3073
    • Pohl E, Holmes RK, Hol WGJ. Crystal structure of a cobalt-activated diphtheria toxin repressor-DNA complex reveals a metal-binding SH3-like domain. J Mol Biol 1999;292:653-667. (Pubitemid 29457326)
    • (1999) Journal of Molecular Biology , vol.292 , Issue.3 , pp. 653-667
    • Pohl, E.1    Holmes, R.K.2    Hol, W.G.J.3
  • 22
    • 0032581662 scopus 로고    scopus 로고
    • Structure of the metal-ion-activated diphtheria toxin repressor/tox operator complex
    • DOI 10.1038/28893
    • White A, Ding X, Vanderspek JC, Murphy JR, Ringe D. Structure of the metal-ion-activated diphtheria toxin repressor/tox operator complex. Nature 1998;394:502-506. (Pubitemid 28373964)
    • (1998) Nature , vol.394 , Issue.6692 , pp. 502-506
    • White, A.1    Ding, X.2    Vanderspek, J.C.3    Murphy, J.R.4    Ringe, D.5
  • 23
    • 0028993911 scopus 로고
    • Three-dimensional structure of the diphtheria toxin repressor in complex with divalent cation co-repressors
    • Qiu X, Verlinde CLMJ, Zhang S, Schmitt MP, Holmes RK, Hol WGJ. Three-dimensional structure of the diphtheria toxin repressor in complex with divalent cation co-repressors. Structure 1995;3:87-100.
    • (1995) Structure , vol.3 , pp. 87-100
    • Qiu, X.1    Clmj, V.2    Zhang, S.3    Schmitt, M.P.4    Holmes, R.K.5    Hol, W.G.J.6
  • 24
    • 0025272639 scopus 로고
    • Current approaches to macromolecular crystallization
    • Mcpherson A. Current approaches to macromolecular crystallization. Eur J Biochem 1990;189:1-23.
    • (1990) Eur J Biochem , vol.189 , pp. 1-23
    • Mcpherson, A.1
  • 25
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • DOI 10.1016/S0076-6879(97)76066-X
    • Otwinowski Z, Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol 1997;276:307-326. (Pubitemid 27085611)
    • (1997) Methods in Enzymology , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 27
    • 0032964481 scopus 로고    scopus 로고
    • Automated protein model building combined with iterative structure refinement
    • DOI 10.1038/8263
    • Perrakis A, Morris R, Lamzin VS. Automated protein model building combined with iterative structure refinement. Nat Struct Biol 1999;6:458-463. (Pubitemid 29218016)
    • (1999) Nature Structural Biology , vol.6 , Issue.5 , pp. 458-463
    • Perrakis, A.1    Morris, R.2    Lamzin, V.S.3
  • 29
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • Emsley P, Cowtan K. Coot: model-building tools for molecular graphics. Acta Crystallogr D 2004;60:2126-2132.
    • (2004) Acta Crystallogr D , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 31
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Higgins D, Thompson J, Gibson T, Thompson JD, Higgins DG, Gibson TJ. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 1994;22:4673-4680. (Pubitemid 24354800)
    • (1994) Nucleic Acids Research , vol.22 , Issue.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 32
    • 0024297354 scopus 로고
    • Multiple sequence alignment with hierarchical clustering
    • Corpet F. Multiple sequence alignment with hierarchical clustering. Nucleic Acids Res 1988;16:10881-10890.
    • (1988) Nucleic Acids Res , vol.16 , pp. 10881-10890
    • Corpet, F.1
  • 33
    • 4444371630 scopus 로고    scopus 로고
    • Crystal structure of an IdeR-DNA complex reveals a conformational change in activated IdeR for base-specific interactions
    • DOI 10.1016/j.jmb.2004.07.083, PII S0022283604009234
    • Wisedchaisri G, Holmes RK, Hol WG. Crystal structure of an IdeRDNA complex reveals a conformational change in activated IdeR for base-specific interactions. J Mol Biol 2004;342:1155-1169. (Pubitemid 39207894)
    • (2004) Journal of Molecular Biology , vol.342 , Issue.4 , pp. 1155-1169
    • Wisedchaisri, G.1    Holmes, R.K.2    Hol, W.G.J.3
  • 35
    • 0032584223 scopus 로고    scopus 로고
    • How Cro and k-repressor distinguish between operators: The structural basis underlying a genetic switch
    • Albright RA, Matthews BW. How Cro and k-repressor distinguish between operators: the structural basis underlying a genetic switch. Proc Natl Acad Sci USA 1998;95:3431-3436.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 3431-3436
    • Albright, R.A.1    Matthews, B.W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.