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Volumn 52, Issue 28, 2013, Pages 4842-4847

Why is the GMN motif conserved in the CorA/Mrs2/Alr1 superfamily of magnesium transport proteins?

Author keywords

[No Author keywords available]

Indexed keywords

EXTRACELLULAR LOOPS; FUNCTIONAL DATAS; MOLECULAR INSIGHTS; OPEN CONFORMATION; SEQUENCE CONSERVATION; STRUCTURE-FUNCTION ANALYSIS; THERMOTOGA MARITIMA; TRANSPORT PROTEINS;

EID: 84880549396     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi4007397     Document Type: Article
Times cited : (22)

References (25)
  • 1
    • 33748031116 scopus 로고    scopus 로고
    • 2+ homeostasis and the CorA translocation cycle
    • 2+ homeostasis and the CorA translocation cycle EMBO J. 25, 3762-3773
    • (2006) EMBO J. , vol.25 , pp. 3762-3773
    • Payandeh, J.1    Pai, E.F.2
  • 3
    • 33746549925 scopus 로고    scopus 로고
    • Crystal structure of a divalent metal ion transporter CorA at 2.9 angstrom resolution
    • Eshaghi, S., Niegowski, D., Kohl, A., Martinez Molina, D., Lesley, S. A., and Nordlund, P. (2006) Crystal structure of a divalent metal ion transporter CorA at 2.9 angstrom resolution Science 313, 354-357
    • (2006) Science , vol.313 , pp. 354-357
    • Eshaghi, S.1    Niegowski, D.2    Kohl, A.3    Martinez Molina, D.4    Lesley, S.A.5    Nordlund, P.6
  • 5
    • 84869223151 scopus 로고    scopus 로고
    • Structural asymmetry in the magnesium channel CorA points to sequential allosteric regulation
    • Pfoh, R., Li, A., Chakrabarti, N., Payandeh, J., Pomes, R., and Pai, E. F. (2012) Structural asymmetry in the magnesium channel CorA points to sequential allosteric regulation Proc. Natl. Acad. Sci. U.S.A. 109, 18809-18814
    • (2012) Proc. Natl. Acad. Sci. U.S.A. , vol.109 , pp. 18809-18814
    • Pfoh, R.1    Li, A.2    Chakrabarti, N.3    Payandeh, J.4    Pomes, R.5    Pai, E.F.6
  • 7
    • 0033601242 scopus 로고    scopus 로고
    • 2+ transport protein of Salmonella typhimurium. Mutagenesis of conserved residues in the second membrane domain
    • 2+ transport protein of Salmonella typhimurium. Mutagenesis of conserved residues in the second membrane domain J. Biol. Chem. 274, 36973-36979
    • (1999) J. Biol. Chem. , vol.274 , pp. 36973-36979
    • Szegedy, M.A.1    Maguire, M.E.2
  • 9
    • 26944487922 scopus 로고    scopus 로고
    • Transport of magnesium and other divalent cations: Evolution of the 2-TM-GxN proteins in the MIT superfamily
    • Knoop, V., Groth-Malonek, M., Gebert, M., Eifler, K., and Weyand, K. (2005) Transport of magnesium and other divalent cations: Evolution of the 2-TM-GxN proteins in the MIT superfamily Mol. Genet. Genomics 274, 205-216
    • (2005) Mol. Genet. Genomics , vol.274 , pp. 205-216
    • Knoop, V.1    Groth-Malonek, M.2    Gebert, M.3    Eifler, K.4    Weyand, K.5
  • 11
    • 84864994769 scopus 로고    scopus 로고
    • The periplasmic loop provides stability to the open state of the CorA magnesium channel
    • Palombo, I., Daley, D. O., and Rapp, M. (2012) The periplasmic loop provides stability to the open state of the CorA magnesium channel J. Biol. Chem. 287, 27547-27555
    • (2012) J. Biol. Chem. , vol.287 , pp. 27547-27555
    • Palombo, I.1    Daley, D.O.2    Rapp, M.3
  • 13
    • 67650173033 scopus 로고    scopus 로고
    • Ligand binding in the conserved interhelical loop of CorA, a magnesium transporter from Mycobacterium tuberculosis
    • Hu, J., Sharma, M., Qin, H., Gao, F. P., and Cross, T. A. (2009) Ligand binding in the conserved interhelical loop of CorA, a magnesium transporter from Mycobacterium tuberculosis J. Biol. Chem. 284, 15619-15628
    • (2009) J. Biol. Chem. , vol.284 , pp. 15619-15628
    • Hu, J.1    Sharma, M.2    Qin, H.3    Gao, F.P.4    Cross, T.A.5
  • 14
    • 19744376674 scopus 로고    scopus 로고
    • Global topology analysis of the Escherichia coli inner membrane proteome
    • Daley, D. O., Rapp, M., Granseth, E., Melen, K., Drew, D., and von Heijne, G. (2005) Global topology analysis of the Escherichia coli inner membrane proteome Science 308, 1321-1323
    • (2005) Science , vol.308 , pp. 1321-1323
    • Daley, D.O.1    Rapp, M.2    Granseth, E.3    Melen, K.4    Drew, D.5    Von Heijne, G.6
  • 18
    • 0020510718 scopus 로고
    • Salmonella typhimurium LT2 strains which are r- m+ for all three chromosomally located systems of DNA restriction and modification
    • Bullas, L. R. and Ryu, J. I. (1983) Salmonella typhimurium LT2 strains which are r- m+ for all three chromosomally located systems of DNA restriction and modification J. Bacteriol. 156, 471-474
    • (1983) J. Bacteriol. , vol.156 , pp. 471-474
    • Bullas, L.R.1    Ryu, J.I.2
  • 19
    • 52649169231 scopus 로고    scopus 로고
    • 2+ channel function affects the virulence of Salmonella enterica serovar typhimurium
    • 2+ channel function affects the virulence of Salmonella enterica serovar typhimurium J. Bacteriol. 190, 6509-6516
    • (2008) J. Bacteriol. , vol.190 , pp. 6509-6516
    • Papp-Wallace, K.M.1    Maguire, M.E.2
  • 20
    • 77954070546 scopus 로고    scopus 로고
    • Control of membrane protein topology by a single C-terminal residue
    • Seppala, S., Slusky, J. S., Lloris-Garcera, P., Rapp, M., and von Heijne, G. (2010) Control of membrane protein topology by a single C-terminal residue Science 328, 1698-1700
    • (2010) Science , vol.328 , pp. 1698-1700
    • Seppala, S.1    Slusky, J.S.2    Lloris-Garcera, P.3    Rapp, M.4    Von Heijne, G.5
  • 21
    • 84860390560 scopus 로고    scopus 로고
    • Penicillin-binding protein 5 can form a homo-oligomeric complex in the inner membrane of Escherichia coli
    • Skoog, K., Bruzell, F. S., Ducroux, A., Hellberg, M., Johansson, H., Lehtio, J., Hogbom, M., and Daley, D. O. (2011) Penicillin-binding protein 5 can form a homo-oligomeric complex in the inner membrane of Escherichia coli Protein Sci. 20, 1520-1529
    • (2011) Protein Sci. , vol.20 , pp. 1520-1529
    • Skoog, K.1    Bruzell, F.S.2    Ducroux, A.3    Hellberg, M.4    Johansson, H.5    Lehtio, J.6    Hogbom, M.7    Daley, D.O.8
  • 22
    • 84857375148 scopus 로고    scopus 로고
    • The Escherichia coli cell division protein ZipA forms homodimers prior to association with FtsZ
    • Skoog, K. and Daley, D. O. (2012) The Escherichia coli cell division protein ZipA forms homodimers prior to association with FtsZ Biochemistry 51, 1407-1415
    • (2012) Biochemistry , vol.51 , pp. 1407-1415
    • Skoog, K.1    Daley, D.O.2
  • 23
    • 0036312670 scopus 로고    scopus 로고
    • Structure, properties and regulation of magnesium transport proteins
    • Kehres, D. G. and Maguire, M. E. (2002) Structure, properties and regulation of magnesium transport proteins BioMetals 15, 261-270
    • (2002) BioMetals , vol.15 , pp. 261-270
    • Kehres, D.G.1    Maguire, M.E.2
  • 25
    • 31044440408 scopus 로고    scopus 로고
    • Residues of the yeast ALR1 protein that are critical for magnesium uptake
    • Lee, J. M. and Gardner, R. C. (2006) Residues of the yeast ALR1 protein that are critical for magnesium uptake Curr. Genet. 49, 7-20
    • (2006) Curr. Genet. , vol.49 , pp. 7
    • Lee, J.M.1    Gardner, R.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.