1rlu
From Proteopedia
(New page: 200px<br /><applet load="1rlu" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rlu, resolution 2.08Å" /> '''Mycobacterium tuberc...) |
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| - | [[Image:1rlu.gif|left|200px]]<br /><applet load="1rlu" size=" | + | [[Image:1rlu.gif|left|200px]]<br /><applet load="1rlu" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1rlu, resolution 2.08Å" /> | caption="1rlu, resolution 2.08Å" /> | ||
'''Mycobacterium tuberculosis FtsZ in complex with GTP-gamma-S'''<br /> | '''Mycobacterium tuberculosis FtsZ in complex with GTP-gamma-S'''<br /> | ||
==Overview== | ==Overview== | ||
| - | We report three crystal structures of the Mycobacterium tuberculosis cell | + | We report three crystal structures of the Mycobacterium tuberculosis cell division protein FtsZ, as the citrate, GDP, and GTPgammaS complexes, determined at 1.89, 2.60, and 2.08A resolution. MtbFtsZ crystallized as a tight, laterally oriented dimer distinct from the longitudinal polymer observed for alphabeta-tubulin. Mutational data on Escherichia coli FtsZ suggest that this dimer interface is important for proper protofilament and "Z-ring" assembly and function. An alpha-to-beta secondary structure conformational switch at the dimer interface is spatially analogous to, and has many of the hallmarks of, the Switch I conformational changes exhibited by G-proteins upon activation. The presence of a gamma-phosphate in the FtsZ active site modulates the conformation of the "tubulin" loop T3 (spatially analogous to the G-protein Switch II); T3 switching upon gamma-phosphate ligation is directly coupled to the alpha-to-beta switch by steric overlap. The dual conformational switches observed here for the first time in an FtsZ link GTP binding and hydrolysis to FtsZ (and tubulin) lateral assembly and Z-ring contraction, and they are suggestive of an underappreciated functional analogy between FtsZ, tubulin and G-proteins. |
==About this Structure== | ==About this Structure== | ||
| - | 1RLU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis] with GSP and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1RLU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis] with <scene name='pdbligand=GSP:'>GSP</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RLU OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Mycobacterium tuberculosis]] | [[Category: Mycobacterium tuberculosis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Borhani, D | + | [[Category: Borhani, D W.]] |
| - | [[Category: DeVito, J | + | [[Category: DeVito, J A.]] |
| - | [[Category: Leung, A | + | [[Category: Leung, A K.W.]] |
| - | [[Category: Reynolds, R | + | [[Category: Reynolds, R C.]] |
| - | [[Category: Ross, L | + | [[Category: Ross, L J.]] |
| - | [[Category: White, E | + | [[Category: White, E L.]] |
[[Category: GOL]] | [[Category: GOL]] | ||
[[Category: GSP]] | [[Category: GSP]] | ||
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[[Category: tubulin]] | [[Category: tubulin]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:52:18 2008'' |
Revision as of 12:52, 21 February 2008
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Mycobacterium tuberculosis FtsZ in complex with GTP-gamma-S
Overview
We report three crystal structures of the Mycobacterium tuberculosis cell division protein FtsZ, as the citrate, GDP, and GTPgammaS complexes, determined at 1.89, 2.60, and 2.08A resolution. MtbFtsZ crystallized as a tight, laterally oriented dimer distinct from the longitudinal polymer observed for alphabeta-tubulin. Mutational data on Escherichia coli FtsZ suggest that this dimer interface is important for proper protofilament and "Z-ring" assembly and function. An alpha-to-beta secondary structure conformational switch at the dimer interface is spatially analogous to, and has many of the hallmarks of, the Switch I conformational changes exhibited by G-proteins upon activation. The presence of a gamma-phosphate in the FtsZ active site modulates the conformation of the "tubulin" loop T3 (spatially analogous to the G-protein Switch II); T3 switching upon gamma-phosphate ligation is directly coupled to the alpha-to-beta switch by steric overlap. The dual conformational switches observed here for the first time in an FtsZ link GTP binding and hydrolysis to FtsZ (and tubulin) lateral assembly and Z-ring contraction, and they are suggestive of an underappreciated functional analogy between FtsZ, tubulin and G-proteins.
About this Structure
1RLU is a Single protein structure of sequence from Mycobacterium tuberculosis with and as ligands. Full crystallographic information is available from OCA.
Reference
Structure of Mycobacterium tuberculosis FtsZ reveals unexpected, G protein-like conformational switches., Leung AK, Lucile White E, Ross LJ, Reynolds RC, DeVito JA, Borhani DW, J Mol Biol. 2004 Sep 17;342(3):953-70. PMID:15342249
Page seeded by OCA on Thu Feb 21 14:52:18 2008
Categories: Mycobacterium tuberculosis | Single protein | Borhani, D W. | DeVito, J A. | Leung, A K.W. | Reynolds, R C. | Ross, L J. | White, E L. | GOL | GSP | Cell cycle | Gtpase | Tubulin
