1w2e
From Proteopedia
(New page: 200px<br /><applet load="1w2e" size="450" color="white" frame="true" align="right" spinBox="true" caption="1w2e, resolution 2.8Å" /> '''THE CRYSTAL STRUCTURE...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1w2e.jpg|left|200px]]<br /><applet load="1w2e" size=" | + | [[Image:1w2e.jpg|left|200px]]<br /><applet load="1w2e" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1w2e, resolution 2.8Å" /> | caption="1w2e, resolution 2.8Å" /> | ||
'''THE CRYSTAL STRUCTURE OF THE BACTERIAL CELL DIVISION PROTEIN ZAPA'''<br /> | '''THE CRYSTAL STRUCTURE OF THE BACTERIAL CELL DIVISION PROTEIN ZAPA'''<br /> | ||
==Overview== | ==Overview== | ||
| - | FtsZ is part of a mid-cell cytokinetic structure termed the Z-ring that | + | FtsZ is part of a mid-cell cytokinetic structure termed the Z-ring that recruits a hierarchy of fission related proteins early in the bacterial cell cycle. The widely conserved ZapA has been shown to interact with FtsZ, to drive its polymerisation and to promote FtsZ filament bundling thereby contributing to the spatio-temporal tuning of the Z-ring. Here, we show the crystal structure of ZapA (11.6 kDa) from Pseudomonas aeruginosa at 2.8 A resolution. The electron density reveals two dimers associating via an extensive C-terminal coiled-coil protrusion to form an elongated anti-parallel tetramer. In solution, ZapA exists in a dimer-tetramer equilibrium that is strongly correlated with concentration. An increase in concentration promotes formation of the higher oligomeric state. The dimer is postulated to be the predominant physiological species although the tetramer could become significant if, as FtsZ is integrated into the Z-ring and is cross-linked, the local concentration of the dimer becomes sufficiently high. We also show that ZapA binds FtsZ with an approximate 1:1 molar stoichiometry and that this interaction provokes dramatic FtsZ polymerisation and inter-filament association as well as yielding filaments, single or bundled, more stable and resistant to collapse. Whilst in vitro dynamics of FtsZ are well characterised, its in vivo arrangement within the ultra-structural architecture of the Z-ring is yet to be determined despite being fundamental to cell division. The ZapA dimer has single 2-fold symmetry whilst the bipolar tetramer displays triple 2-fold symmetry. Given the symmetry of these ZapA oligomers and the polar nature of FtsZ filaments, the structure of ZapA carries novel implications for the inherent architecture of the Z-ring in vivo. |
==About this Structure== | ==About this Structure== | ||
| - | 1W2E is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http:// | + | 1W2E is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W2E OCA]. |
==Reference== | ==Reference== | ||
| Line 13: | Line 13: | ||
[[Category: Pseudomonas aeruginosa]] | [[Category: Pseudomonas aeruginosa]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Low, H | + | [[Category: Low, H H.]] |
[[Category: Lowe, J.]] | [[Category: Lowe, J.]] | ||
| - | [[Category: Moncrieffe, M | + | [[Category: Moncrieffe, M C.]] |
[[Category: bacterial cell division]] | [[Category: bacterial cell division]] | ||
[[Category: ftsz modulator]] | [[Category: ftsz modulator]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:39:48 2008'' |
Revision as of 13:39, 21 February 2008
|
THE CRYSTAL STRUCTURE OF THE BACTERIAL CELL DIVISION PROTEIN ZAPA
Overview
FtsZ is part of a mid-cell cytokinetic structure termed the Z-ring that recruits a hierarchy of fission related proteins early in the bacterial cell cycle. The widely conserved ZapA has been shown to interact with FtsZ, to drive its polymerisation and to promote FtsZ filament bundling thereby contributing to the spatio-temporal tuning of the Z-ring. Here, we show the crystal structure of ZapA (11.6 kDa) from Pseudomonas aeruginosa at 2.8 A resolution. The electron density reveals two dimers associating via an extensive C-terminal coiled-coil protrusion to form an elongated anti-parallel tetramer. In solution, ZapA exists in a dimer-tetramer equilibrium that is strongly correlated with concentration. An increase in concentration promotes formation of the higher oligomeric state. The dimer is postulated to be the predominant physiological species although the tetramer could become significant if, as FtsZ is integrated into the Z-ring and is cross-linked, the local concentration of the dimer becomes sufficiently high. We also show that ZapA binds FtsZ with an approximate 1:1 molar stoichiometry and that this interaction provokes dramatic FtsZ polymerisation and inter-filament association as well as yielding filaments, single or bundled, more stable and resistant to collapse. Whilst in vitro dynamics of FtsZ are well characterised, its in vivo arrangement within the ultra-structural architecture of the Z-ring is yet to be determined despite being fundamental to cell division. The ZapA dimer has single 2-fold symmetry whilst the bipolar tetramer displays triple 2-fold symmetry. Given the symmetry of these ZapA oligomers and the polar nature of FtsZ filaments, the structure of ZapA carries novel implications for the inherent architecture of the Z-ring in vivo.
About this Structure
1W2E is a Single protein structure of sequence from Pseudomonas aeruginosa. Full crystallographic information is available from OCA.
Reference
The crystal structure of ZapA and its modulation of FtsZ polymerisation., Low HH, Moncrieffe MC, Lowe J, J Mol Biol. 2004 Aug 13;341(3):839-52. PMID:15288790
Page seeded by OCA on Thu Feb 21 15:39:48 2008
