1w5f: Difference between revisions

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==Overview==

The prokaryotic tubulin homolog FtsZ polymerizes into a ring structure, essential for bacterial cell division. We have used refolded FtsZ to, crystallize a tubulin-like protofilament. The N- and C-terminal domains of, two consecutive subunits in the filament assemble to form the GTPase site, with the C-terminal domain providing water-polarizing residues. A, domain-swapped structure of FtsZ and biochemical data on purified N- and, C-terminal domains show that they are independent. This leads to a model, of how FtsZ and tubulin polymerization evolved by fusing two domains. In, polymerized tubulin, the nucleotide-binding pocket is occluded, which, leads to nucleotide exchange being the rate-limiting step and to dynamic, instability. In our FtsZ filament structure the nucleotide is, exchangeable, explaining why, in this filament, nucleotide hydrolysis is, the rate-limiting step during FtsZ polymerization. Furthermore, crystal, structures of FtsZ in different nucleotide states reveal notably few, differences.

The prokaryotic tubulin homolog FtsZ polymerizes into a ring structure essential for bacterial cell division. We have used refolded FtsZ to crystallize a tubulin-like protofilament. The N- and C-terminal domains of two consecutive subunits in the filament assemble to form the GTPase site, with the C-terminal domain providing water-polarizing residues. A domain-swapped structure of FtsZ and biochemical data on purified N- and C-terminal domains show that they are independent. This leads to a model of how FtsZ and tubulin polymerization evolved by fusing two domains. In polymerized tubulin, the nucleotide-binding pocket is occluded, which leads to nucleotide exchange being the rate-limiting step and to dynamic instability. In our FtsZ filament structure the nucleotide is exchangeable, explaining why, in this filament, nucleotide hydrolysis is the rate-limiting step during FtsZ polymerization. Furthermore, crystal structures of FtsZ in different nucleotide states reveal notably few differences.

==About this Structure==

Line 13:

[[Category: Single protein]]

[[Category: Thermotoga maritima]]

[[Category: Cordell, S.C.]]

[[Category: Cordell, S C.]]

[[Category: Lowe, J.]]

[[Category: Oliva, M.A.]]

[[Category: Oliva, M A.]]

[[Category: G2P]]

[[Category: MG]]

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[[Category: z-ring]]

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@@ Line 4: / Line 4: @@
 ==Overview==
-The prokaryotic tubulin homolog FtsZ polymerizes into a ring structure, essential for bacterial cell division. We have used refolded FtsZ to, crystallize a tubulin-like protofilament. The N- and C-terminal domains of, two consecutive subunits in the filament assemble to form the GTPase site, with the C-terminal domain providing water-polarizing residues. A, domain-swapped structure of FtsZ and biochemical data on purified N- and, C-terminal domains show that they are independent. This leads to a model, of how FtsZ and tubulin polymerization evolved by fusing two domains. In, polymerized tubulin, the nucleotide-binding pocket is occluded, which, leads to nucleotide exchange being the rate-limiting step and to dynamic, instability. In our FtsZ filament structure the nucleotide is, exchangeable, explaining why, in this filament, nucleotide hydrolysis is, the rate-limiting step during FtsZ polymerization. Furthermore, crystal, structures of FtsZ in different nucleotide states reveal notably few, differences.
+The prokaryotic tubulin homolog FtsZ polymerizes into a ring structure essential for bacterial cell division. We have used refolded FtsZ to crystallize a tubulin-like protofilament. The N- and C-terminal domains of two consecutive subunits in the filament assemble to form the GTPase site, with the C-terminal domain providing water-polarizing residues. A domain-swapped structure of FtsZ and biochemical data on purified N- and C-terminal domains show that they are independent. This leads to a model of how FtsZ and tubulin polymerization evolved by fusing two domains. In polymerized tubulin, the nucleotide-binding pocket is occluded, which leads to nucleotide exchange being the rate-limiting step and to dynamic instability. In our FtsZ filament structure the nucleotide is exchangeable, explaining why, in this filament, nucleotide hydrolysis is the rate-limiting step during FtsZ polymerization. Furthermore, crystal structures of FtsZ in different nucleotide states reveal notably few differences.
 ==About this Structure==
@@ Line 13: / Line 13: @@
 [[Category: Single protein]]
 [[Category: Thermotoga maritima]]
-[[Category: Cordell, S.C.]]
+[[Category: Cordell, S C.]]
 [[Category: Lowe, J.]]
-[[Category: Oliva, M.A.]]
+[[Category: Oliva, M A.]]
 [[Category: G2P]]
 [[Category: MG]]
@@ Line 31: / Line 31: @@
 [[Category: z-ring]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb  3 10:19:34 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:40:40 2008''