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Volumn 289, Issue 32, 2014, Pages 22377-22384

Structural insights into higher order assembly and function of the bacterial micro compartment protein PduA

Author keywords

[No Author keywords available]

Indexed keywords

CYTOLOGY;

EID: 84905867273     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.569285     Document Type: Article
Times cited : (62)

References (32)
  • 1
    • 0032822281 scopus 로고    scopus 로고
    • The propanediol utilization (pdu) operon of Salmonella enterica serovar Typhimurium LT2 includes genes necessary for formation of polyhedral organelles involved in coenzyme B12-dependent 1, 2-propanediol degradation
    • Bobik, T. A., Havemann, G. D., Busch, R. J., Williams, D. S., and Aldrich, H. C. (1999) The propanediol utilization (pdu) operon of Salmonella enterica serovar Typhimurium LT2 includes genes necessary for formation of polyhedral organelles involved in coenzyme B12-dependent 1, 2-propanediol degradation. J. Bacteriol. 181, 5967-5975
    • (1999) J. Bacteriol. , vol.181 , pp. 5967-5975
    • Bobik, T.A.1    Havemann, G.D.2    Busch, R.J.3    Williams, D.S.4    Aldrich, H.C.5
  • 2
    • 0032408245 scopus 로고    scopus 로고
    • Sequence homologs of the carboxysomal polypeptide CsoS1 of the thiobacilli are present in cyanobacteria and enteric bacteria that form carboxysomes: Polyhedral bodies
    • Shively, J. M., Bradburne, C. E., Aldrich, H. C., Bobik, T. A., Mehlman, J. L., Jin, S., and Baker, S. H. (1998) Sequence homologs of the carboxysomal polypeptide CsoS1 of the thiobacilli are present in cyanobacteria and enteric bacteria that form carboxysomes: polyhedral bodies. Can. J. Bot. 76, 906-916
    • (1998) Can. J. Bot. , vol.76 , pp. 906-916
    • Shively, J.M.1    Bradburne, C.E.2    Aldrich, H.C.3    Bobik, T.A.4    Mehlman, J.L.5    Jin, S.6    Baker, S.H.7
  • 3
    • 46049098363 scopus 로고    scopus 로고
    • Lactobacillus reuteri DSM 20016 produces cobalamin-dependent diol dehydratase in metabolosomes and metabolizes 1,2-propanediol by disproportionation
    • Sriramulu, D. D., Liang, M., Hernandez-Romero, D., Raux-Deery, E., Lünsdorf, H., Parsons, J. B., Warren, M. J., and Prentice, M. B. (2008) Lactobacillus reuteri DSM 20016 produces cobalamin-dependent diol dehydratase in metabolosomes and metabolizes 1,2-propanediol by disproportionation. J. Bacteriol. 190, 4559-4567
    • (2008) J. Bacteriol. , vol.190 , pp. 4559-4567
    • Sriramulu, D.D.1    Liang, M.2    Hernandez-Romero, D.3    Raux-Deery, E.4    Lünsdorf, H.5    Parsons, J.B.6    Warren, M.J.7    Prentice, M.B.8
  • 4
    • 0016138224 scopus 로고
    • Characterization of a phagelike particle from cells of Nitrobacter. I. Host-particle correlation and particle isolation (author's transl)
    • Bock, E., Düvel, D. and Peters, K. R. (1974) [Characterization of a phagelike particle from cells of Nitrobacter. I. Host-particle correlation and particle isolation (author's transl)]. Arch. Microbiol. 97, 115-127
    • (1974) Arch. Microbiol. , vol.97 , pp. 115-127
    • Bock, E.1    Düvel, D.2    Peters, K.R.3
  • 6
    • 28044459168 scopus 로고    scopus 로고
    • Minimal functions and physiological conditions required for growth of Salmonella enterica on ethanolamine in the absence of the metabolosome
    • Brinsmade, S. R., Paldon, T., and Escalante-Semerena, J. C. (2005) Minimal functions and physiological conditions required for growth of Salmonella enterica on ethanolamine in the absence of the metabolosome. J. Bacteriol. 187, 8039-8046
    • (2005) J. Bacteriol. , vol.187 , pp. 8039-8046
    • Brinsmade, S.R.1    Paldon, T.2    Escalante-Semerena, J.C.3
  • 7
    • 84874058227 scopus 로고    scopus 로고
    • Using comparative genomics to uncover new kinds of protein-based metabolic organelles in bacteria
    • Jorda, J., Lopez, D., Wheatley, N. M., and Yeates, T. O. (2013) Using comparative genomics to uncover new kinds of protein-based metabolic organelles in bacteria. Protein Sci. 22, 179-195
    • (2013) Protein Sci. , vol.22 , pp. 179-195
    • Jorda, J.1    Lopez, D.2    Wheatley, N.M.3    Yeates, T.O.4
  • 9
    • 0028944586 scopus 로고
    • Ethanolamine utilization in Salmonella typhimurium: Nucleotide sequence, protein expression, and mutational analysis of the cchA cchB eutE eutJ eutG eutH gene cluster
    • Stojiljkovic, I., Bäumler, A. J. and Heffron, F. (1995) Ethanolamine utilization in Salmonella typhimurium: nucleotide sequence, protein expression, and mutational analysis of the cchA cchB eutE eutJ eutG eutH gene cluster. J. Bacteriol. 177, 1357-1366
    • (1995) J. Bacteriol. , vol.177 , pp. 1357-1366
    • Stojiljkovic, I.1    Bäumler, A.J.2    Heffron, F.3
  • 10
    • 0031050994 scopus 로고    scopus 로고
    • Genetic characterization of the pdu operon: Use of 1,2-propanediol in Salmonella typhimurium
    • Walter, D., Ailion, M., and Roth, J. (1997) Genetic characterization of the pdu operon: use of 1,2-propanediol in Salmonella typhimurium. J. Bacteriol. 179, 1013-1022
    • (1997) J. Bacteriol. , vol.179 , pp. 1013-1022
    • Walter, D.1    Ailion, M.2    Roth, J.3
  • 12
    • 70350096554 scopus 로고    scopus 로고
    • Structure of a trimeric bacterial microcompartment shell protein, EtuB, associated with ethanol utilization in Clostridium kluyveri
    • Heldt, D., Frank, S., Seyedarabi, A., Ladikis, D., Parsons, J. B., Warren, M. J., and Pickersgill, R. W. (2009) Structure of a trimeric bacterial microcompartment shell protein, EtuB, associated with ethanol utilization in Clostridium kluyveri. Biochem. J. 423, 199-207
    • (2009) Biochem. J. , vol.423 , pp. 199-207
    • Heldt, D.1    Frank, S.2    Seyedarabi, A.3    Ladikis, D.4    Parsons, J.B.5    Warren, M.J.6    Pickersgill, R.W.7
  • 14
    • 79952178155 scopus 로고    scopus 로고
    • Structure of PduT, a trimeric bacterial microcompartment protein with a 4Fe-4S cluster-binding site
    • Pang, A., Warren, M. J., and Pickersgill, R. W. (2011) Structure of PduT, a trimeric bacterial microcompartment protein with a 4Fe-4S cluster-binding site. Acta Crystallogr. D Biol. Crystallogr. 67, 91-96
    • (2011) Acta Crystallogr. D Biol. Crystallogr. , vol.67 , pp. 91-96
    • Pang, A.1    Warren, M.J.2    Pickersgill, R.W.3
  • 15
    • 0042389658 scopus 로고    scopus 로고
    • Protein content of polyhedral organelles involved in coenzyme B12-dependent degradation of 1,2-propanediol in Salmonella enterica serovar Typhimurium LT2
    • Havemann, G. D., and Bobik, T. A. (2003) Protein content of polyhedral organelles involved in coenzyme B12-dependent degradation of 1,2-propanediol in Salmonella enterica serovar Typhimurium LT2. J. Bacteriol. 185, 5086-5095
    • (2003) J. Bacteriol. , vol.185 , pp. 5086-5095
    • Havemann, G.D.1    Bobik, T.A.2
  • 17
    • 77950906711 scopus 로고    scopus 로고
    • Synthesis of empty bacterial microcompartments, directed organelle protein incorporation, and evidence of filamentassociated organelle movement
    • Parsons, J. B., Frank, S., Bhella, D., Liang, M., Prentice, M. B., Mulvihill, D. P., Warren, M. J. (2010) Synthesis of empty bacterial microcompartments, directed organelle protein incorporation, and evidence of filamentassociated organelle movement. Mol. Cell 38, 305-315
    • (2010) Mol. Cell , vol.38 , pp. 305-315
    • Parsons, J.B.1    Frank, S.2    Bhella, D.3    Liang, M.4    Prentice, M.B.5    Mulvihill, D.P.6    Warren, M.J.7
  • 18
    • 79952367508 scopus 로고    scopus 로고
    • Genetic analysis of the protein shell of the microcompartments involved in coenzyme B-12-dependent 1,2-propanediol degradation by Salmonella
    • Cheng, S., Sinha, S., Fan, C., Liu, Y., and Bobik, T. A. (2011) Genetic analysis of the protein shell of the microcompartments involved in coenzyme B-12-dependent 1,2-propanediol degradation by Salmonella. J. Bacteriol. 193, 1385-1392
    • (2011) J. Bacteriol. , vol.193 , pp. 1385-1392
    • Cheng, S.1    Sinha, S.2    Fan, C.3    Liu, Y.4    Bobik, T.A.5
  • 19
    • 78549246253 scopus 로고    scopus 로고
    • Structural insight into the mechanisms of transport across the Salmonella enterica Pdu microcompartment shell
    • Crowley, C. S., Cascio, D., Sawaya, M. R., Kopstein, J. S., Bobik, T. A., and Yeates, T. O. (2010) Structural insight into the mechanisms of transport across the Salmonella enterica Pdu microcompartment shell. J. Biol. Chem. 285, 37838-37846
    • (2010) J. Biol. Chem. , vol.285 , pp. 37838-37846
    • Crowley, C.S.1    Cascio, D.2    Sawaya, M.R.3    Kopstein, J.S.4    Bobik, T.A.5    Yeates, T.O.6
  • 20
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, Number 4
    • Collaborative Computational Project, Number 4 (1994) The CCP4 suite: programs for protein crystallography. Acta Crystallogr.DBiol. Crystallogr. 50, 760-763
    • (1994) Acta Crystallogr.DBiol. Crystallogr. , vol.50 , pp. 760-763
  • 21
    • 33947304702 scopus 로고    scopus 로고
    • PyMOL: A communications tool for computational models
    • DeLano, W. L., and Lam, J. W. (2005) PyMOL: a communications tool for computational models. Abstr. Papers Am. Chem. Soc. 230, 254-COMP
    • (2005) Abstr. Papers Am. Chem. Soc. , vol.230
    • Delano, W.L.1    Lam, J.W.2
  • 27
    • 0000560808 scopus 로고    scopus 로고
    • MOLREP: An automated program for molecular replacement
    • Vagin, A., and Teplyakov, A. (1997) MOLREP: an automated program for molecular replacement. J. Appl. Crystallogr. 30, 1022-1025
    • (1997) J. Appl. Crystallogr. , vol.30 , pp. 1022-1025
    • Vagin, A.1    Teplyakov, A.2
  • 30
    • 0000243829 scopus 로고
    • Procheck: A program to check the stereochemical quality of protein structures
    • Laskowski, R. A., MacArthur, M. W., Moss, D. S., and Thornton, J. M. (1993) Procheck: a program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26, 283-291
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    Macarthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 31
    • 84869431601 scopus 로고    scopus 로고
    • Substrate channels revealed in the trimeric Lactobacillus reuteri bacterial microcompartment shell protein PduB
    • Pang, A., Liang, M., Prentice, M. B., and Pickersgill, R. W. (2012) Substrate channels revealed in the trimeric Lactobacillus reuteri bacterial microcompartment shell protein PduB. Acta Crystallogr. D Biol. Crystallogr. 68, 1642-1652
    • (2012) Acta Crystallogr. D Biol. Crystallogr. , vol.68 , pp. 1642-1652
    • Pang, A.1    Liang, M.2    Prentice, M.B.3    Pickersgill, R.W.4
  • 32
    • 84872197140 scopus 로고    scopus 로고
    • Bacterial microcompartments moving into a synthetic biological world
    • Frank, S., Lawrence, A. D., Prentice, M. B., and Warren, M. J. (2013) Bacterial microcompartments moving into a synthetic biological world. J. Biotechnol. 163, 273-279
    • (2013) J. Biotechnol. , vol.163 , pp. 273-279
    • Frank, S.1    Lawrence, A.D.2    Prentice, M.B.3    Warren, M.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.