1w58
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1w58 |SIZE=350|CAPTION= <scene name='initialview01'>1w58</scene>, resolution 2.5Å | |PDB= 1w58 |SIZE=350|CAPTION= <scene name='initialview01'>1w58</scene>, resolution 2.5Å | ||
|SITE= <scene name='pdbsite=AC1:Mg+Binding+Site+For+Chain+1'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Mg+Binding+Site+For+Chain+1'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=G2P:PHOSPHOMETHYLPHOSPHONIC+ACID+GUANYLATE+ESTER'>G2P</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1w58 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w58 OCA], [http://www.ebi.ac.uk/pdbsum/1w58 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1w58 RCSB]</span> | ||
}} | }} | ||
| Line 25: | Line 28: | ||
[[Category: Lowe, J.]] | [[Category: Lowe, J.]] | ||
[[Category: Oliva, M A.]] | [[Category: Oliva, M A.]] | ||
| - | [[Category: G2P]] | ||
| - | [[Category: MG]] | ||
[[Category: cell division]] | [[Category: cell division]] | ||
[[Category: cell division protein]] | [[Category: cell division protein]] | ||
| Line 37: | Line 38: | ||
[[Category: tubulin]] | [[Category: tubulin]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:31:22 2008'' |
Revision as of 21:31, 30 March 2008
| |||||||
| , resolution 2.5Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
FTSZ GMPCPP SOAK I213 (M. JANNASCHII)
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.
About this Structure
1W58 is a Single protein structure of sequence from Methanocaldococcus jannaschii. Full crystallographic information is available from OCA.
Reference
Structural insights into FtsZ protofilament formation., Oliva MA, Cordell SC, Lowe J, Nat Struct Mol Biol. 2004 Dec;11(12):1243-50. Epub 2004 Nov 21. PMID:15558053
Page seeded by OCA on Mon Mar 31 00:31:22 2008
