X-ray Crystallographic Analysis of MinC N-Terminal Domain from Escherichia coli
MinC plays an important role in bacterial cell division
system by inhibiting FtsZ assembly. However, the molecular
mechanism of the action is poorly understood. E. coli MinC Nterminus
domain was purified and crystallized using 1.4 M sodium
citrate pH 6.5 as a precipitant. X-ray diffraction data was collected
and processed to 2.3 Å from a native crystal. The crystal belonged to
space group P212121, with the unit cell parameters a = 52.7, b = 54.0,
c = 64.7 Å. Assuming the presence of two molecules in the
asymmetric unit, the Matthews coefficient value is 1.94 Å3 Da-1,
which corresponds to a solvent content of 36.5%. The overall
structure of MinCN is observed as a dimer form through anti-parallel
ß-strand interaction.
[1] Lutkenhaus, J. "Assembly dynamics of the bacterial MinCDE system
and spatial regulation of the Z ring", (2007). Annu. Rev. Biochem., 76,
539-562.
[2] Dajkovic, A. and Lutkenhaus, J. "Z ring as executor of bacterial cell
division", (2006) J. Mol. Microbiol. Biotechnol., 11, 140-151.
[3] Lutkenhaus, J. "The regulation of bacterial cell division: a time and
place for it", (1998) Curr. Opin. Microbiol., 1, 210-215.
[4] Yu, X.-C. and Margolin, W. "FtsZ ring clusters in min and partition
mutants: role of both the Min system and the nucleoid in regulating FtsZ
ring localization", (1999) Mol. Microbiol., 32, 315-326.
[5] de Boer, P. A., Crossley, R. E. and Rothfield, L. I. "A division inhibitor
and a topological specificity factor coded for by the minicell locus
determine proper placement of the division septum in E. coli", (1989)
Cell, 56, 641-649.
[6] Rothfield, L., Justice, S. and Garcia-Lara, J." Bacterial cell division",
(1999) Annu. Rev. Genet., 33, 423-448.
[7] Hu, Z. and Lutkenhaus, J. "Topological regulation of cell division in
Escherichia coli involves rapid pole to pole oscillation of the division
inhibitor MinC under the control of MinD and MinE", (1999) Mol.
Microbiol., 34, 82-90.
[8] Raskin, D. M. and de Boer, P. A. "Rapid pole-to-pole oscillation of a
protein required for directing division to the middle of Escherichia coli",
(1999) Proc. Natl. Acad. Sci USA, 96, 4971-4976.
[9] Hu, Z., Mukherjee, A., Pichoff, S. and Lutkenhaus, J. "The MinC
component of the division site selection system in Escherichia coli
interacts with FtsZ to prevent polymerization", (1999) Proc. Natl. Acad.
Sci. USA, 96, 14819-14824.
[10] Raskin, D. M. and de Boer, P. A. "MinDE-dependent pole-to-pole
oscillation of division inhibitor MinC in Escherichia coli", (1999) J.
Bacteriol., 181, 6419-6424.
[11] Huang, J., Cao, C. and Lutkenhaus, J. "Interaction between FtsZ and
inhibitors of cell division", (1996) J. Bacteriol., 178, 5080-5085.
[12] King, G. F., Shih, Y. L., Maciejewski, M. W., Bains, N. P., Pan, B.,
Rowland, S. L., Mullen, G. P. and Rothfield, L. I. "Structural basis for
the topological specificity function of MinE", (2000) Nat. Struct. Biol.,
7, 1013-1017.
[13] Shen, B. and Lutkenhaus, J. "The conserved C-terminal tail of FtsZ is
required for the septal localization and division inhibitory activity of
MinC(C)/MinD", (2009) Mol. Microbiol., 72, 410-424.
[14] Dajkovic, A., Lan, G., Sun, S. X., Wirtz, D. and Lutkenhaus, J. "MinC
spatially controls bacterial cytokinesis by antagonizing the scaffolding
function of FtsZ", (2008) Curr. Biol., 18, 235-244.
[15] Hu, Z. and Lutkenhaus, J. "Analysis of MinC reveals two independent
domains involved in interaction with MinD and FtsZ", (2000) J.
Bacteriol., 182, 3965-3971.
[16] Otwinowski, Z. and Minor, W. "Processing of X-ray diffraction data
collected in the oscillation mode", (1997) Methods Enzymol., 276, 307-
326.
[17] Matthews, B. W. "Solvent content of protein crystals", (1968) J. Mol.
Biol., 33, 491-497.
[18] McCoy, A. J., Grosse-Kunstleve R. W., Storoni, L. C. and Read, R. J.
"Likelihood-enhanced fast translation functions", (2005) Acta
Crystallogr. D. Biol. Crystallogr., 61, 458-464.
[19] Emsley, P. & Cowtan, K. "Coot: model-building tools for molecular
graphics", (2004) Acta Crystallogr. D., 60, 2126-2132.
[20] Br├╝nger, A. T., Adams, P. D., Clore, G. M., Delano, W. L., Gros, P.,
Grosse-Kunstleve, R. W. et al. "Crystallography and NMR systems: a
new software suite for macromolecular structure determination",
(1998)Acta Crystallogr. D., 54, 905-921.
[21] Murshudov, G. N.,Vagin, A.A. and Dodson,E.J. "Refinement of
macromolecular structures by the maximum-likelihood method", (1997)
Acta Crystallogr. D., 53, 240-255.
[1] Lutkenhaus, J. "Assembly dynamics of the bacterial MinCDE system
and spatial regulation of the Z ring", (2007). Annu. Rev. Biochem., 76,
539-562.
[2] Dajkovic, A. and Lutkenhaus, J. "Z ring as executor of bacterial cell
division", (2006) J. Mol. Microbiol. Biotechnol., 11, 140-151.
[3] Lutkenhaus, J. "The regulation of bacterial cell division: a time and
place for it", (1998) Curr. Opin. Microbiol., 1, 210-215.
[4] Yu, X.-C. and Margolin, W. "FtsZ ring clusters in min and partition
mutants: role of both the Min system and the nucleoid in regulating FtsZ
ring localization", (1999) Mol. Microbiol., 32, 315-326.
[5] de Boer, P. A., Crossley, R. E. and Rothfield, L. I. "A division inhibitor
and a topological specificity factor coded for by the minicell locus
determine proper placement of the division septum in E. coli", (1989)
Cell, 56, 641-649.
[6] Rothfield, L., Justice, S. and Garcia-Lara, J." Bacterial cell division",
(1999) Annu. Rev. Genet., 33, 423-448.
[7] Hu, Z. and Lutkenhaus, J. "Topological regulation of cell division in
Escherichia coli involves rapid pole to pole oscillation of the division
inhibitor MinC under the control of MinD and MinE", (1999) Mol.
Microbiol., 34, 82-90.
[8] Raskin, D. M. and de Boer, P. A. "Rapid pole-to-pole oscillation of a
protein required for directing division to the middle of Escherichia coli",
(1999) Proc. Natl. Acad. Sci USA, 96, 4971-4976.
[9] Hu, Z., Mukherjee, A., Pichoff, S. and Lutkenhaus, J. "The MinC
component of the division site selection system in Escherichia coli
interacts with FtsZ to prevent polymerization", (1999) Proc. Natl. Acad.
Sci. USA, 96, 14819-14824.
[10] Raskin, D. M. and de Boer, P. A. "MinDE-dependent pole-to-pole
oscillation of division inhibitor MinC in Escherichia coli", (1999) J.
Bacteriol., 181, 6419-6424.
[11] Huang, J., Cao, C. and Lutkenhaus, J. "Interaction between FtsZ and
inhibitors of cell division", (1996) J. Bacteriol., 178, 5080-5085.
[12] King, G. F., Shih, Y. L., Maciejewski, M. W., Bains, N. P., Pan, B.,
Rowland, S. L., Mullen, G. P. and Rothfield, L. I. "Structural basis for
the topological specificity function of MinE", (2000) Nat. Struct. Biol.,
7, 1013-1017.
[13] Shen, B. and Lutkenhaus, J. "The conserved C-terminal tail of FtsZ is
required for the septal localization and division inhibitory activity of
MinC(C)/MinD", (2009) Mol. Microbiol., 72, 410-424.
[14] Dajkovic, A., Lan, G., Sun, S. X., Wirtz, D. and Lutkenhaus, J. "MinC
spatially controls bacterial cytokinesis by antagonizing the scaffolding
function of FtsZ", (2008) Curr. Biol., 18, 235-244.
[15] Hu, Z. and Lutkenhaus, J. "Analysis of MinC reveals two independent
domains involved in interaction with MinD and FtsZ", (2000) J.
Bacteriol., 182, 3965-3971.
[16] Otwinowski, Z. and Minor, W. "Processing of X-ray diffraction data
collected in the oscillation mode", (1997) Methods Enzymol., 276, 307-
326.
[17] Matthews, B. W. "Solvent content of protein crystals", (1968) J. Mol.
Biol., 33, 491-497.
[18] McCoy, A. J., Grosse-Kunstleve R. W., Storoni, L. C. and Read, R. J.
"Likelihood-enhanced fast translation functions", (2005) Acta
Crystallogr. D. Biol. Crystallogr., 61, 458-464.
[19] Emsley, P. & Cowtan, K. "Coot: model-building tools for molecular
graphics", (2004) Acta Crystallogr. D., 60, 2126-2132.
[20] Br├╝nger, A. T., Adams, P. D., Clore, G. M., Delano, W. L., Gros, P.,
Grosse-Kunstleve, R. W. et al. "Crystallography and NMR systems: a
new software suite for macromolecular structure determination",
(1998)Acta Crystallogr. D., 54, 905-921.
[21] Murshudov, G. N.,Vagin, A.A. and Dodson,E.J. "Refinement of
macromolecular structures by the maximum-likelihood method", (1997)
Acta Crystallogr. D., 53, 240-255.
@article{"International Journal of Biological, Life and Agricultural Sciences:54820", author = "Jun Yop An and Kyoung Ryoung Park and Jung-Gyu Lee and Hyung-Seop Youn and Jung-Yeon Kang and Gil Bu Kang and Soo Hyun Eom", title = "X-ray Crystallographic Analysis of MinC N-Terminal Domain from Escherichia coli", abstract = "MinC plays an important role in bacterial cell division
system by inhibiting FtsZ assembly. However, the molecular
mechanism of the action is poorly understood. E. coli MinC Nterminus
domain was purified and crystallized using 1.4 M sodium
citrate pH 6.5 as a precipitant. X-ray diffraction data was collected
and processed to 2.3 Å from a native crystal. The crystal belonged to
space group P212121, with the unit cell parameters a = 52.7, b = 54.0,
c = 64.7 Å. Assuming the presence of two molecules in the
asymmetric unit, the Matthews coefficient value is 1.94 Å3 Da-1,
which corresponds to a solvent content of 36.5%. The overall
structure of MinCN is observed as a dimer form through anti-parallel
ß-strand interaction.", keywords = "MinC, Cell division, Crystallization.", volume = "4", number = "8", pages = "560-4", }
