1l0o
From Proteopedia
(New page: 200px<br /><applet load="1l0o" size="450" color="white" frame="true" align="right" spinBox="true" caption="1l0o, resolution 2.9Å" /> '''Crystal Structure of ...) |
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| - | [[Image:1l0o.gif|left|200px]]<br /><applet load="1l0o" size=" | + | [[Image:1l0o.gif|left|200px]]<br /><applet load="1l0o" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1l0o, resolution 2.9Å" /> | caption="1l0o, resolution 2.9Å" /> | ||
'''Crystal Structure of the Bacillus stearothermophilus Anti-Sigma Factor SpoIIAB with the Sporulation Sigma Factor SigmaF'''<br /> | '''Crystal Structure of the Bacillus stearothermophilus Anti-Sigma Factor SpoIIAB with the Sporulation Sigma Factor SigmaF'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Cell type-specific transcription during Bacillus sporulation is | + | Cell type-specific transcription during Bacillus sporulation is established by sigmaF. SpoIIAB is an anti-sigma that binds and negatively regulates sigmaF, as well as a serine kinase that phosphorylates and inactivates the anti-anti-sigma SpoIIAA. The crystal structure of sigmaF bound to the SpoIIAB dimer in the low-affinity, ADP form has been determined at 2.9 A resolution. SpoIIAB adopts the GHKL superfamily fold of ATPases and histidine kinases. A domain of sigmaF contacts both SpoIIAB monomers, while 80% of the sigma factor is disordered. The interaction occludes an RNA polymerase binding surface of sigmaF, explaining the SpoIIAB anti-sigma activity. The structure also explains the specificity of SpoIIAB for its target sigma factors and, in combination with genetic and biochemical data, provides insight into the mechanism of SpoIIAA anti-anti-sigma activity. |
==About this Structure== | ==About this Structure== | ||
| - | 1L0O is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus] with MG and ADP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1L0O is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=ADP:'>ADP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L0O OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Geobacillus stearothermophilus]] | [[Category: Geobacillus stearothermophilus]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Campbell, E | + | [[Category: Campbell, E A.]] |
| - | [[Category: Darst, S | + | [[Category: Darst, S A.]] |
[[Category: Masuda, S.]] | [[Category: Masuda, S.]] | ||
[[Category: Muzzin, O.]] | [[Category: Muzzin, O.]] | ||
| - | [[Category: Olson, C | + | [[Category: Olson, C A.]] |
| - | [[Category: Sun, J | + | [[Category: Sun, J L.]] |
[[Category: Wang, S.]] | [[Category: Wang, S.]] | ||
[[Category: ADP]] | [[Category: ADP]] | ||
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[[Category: helix-turn-helix]] | [[Category: helix-turn-helix]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:40:00 2008'' |
Revision as of 11:40, 21 February 2008
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Crystal Structure of the Bacillus stearothermophilus Anti-Sigma Factor SpoIIAB with the Sporulation Sigma Factor SigmaF
Overview
Cell type-specific transcription during Bacillus sporulation is established by sigmaF. SpoIIAB is an anti-sigma that binds and negatively regulates sigmaF, as well as a serine kinase that phosphorylates and inactivates the anti-anti-sigma SpoIIAA. The crystal structure of sigmaF bound to the SpoIIAB dimer in the low-affinity, ADP form has been determined at 2.9 A resolution. SpoIIAB adopts the GHKL superfamily fold of ATPases and histidine kinases. A domain of sigmaF contacts both SpoIIAB monomers, while 80% of the sigma factor is disordered. The interaction occludes an RNA polymerase binding surface of sigmaF, explaining the SpoIIAB anti-sigma activity. The structure also explains the specificity of SpoIIAB for its target sigma factors and, in combination with genetic and biochemical data, provides insight into the mechanism of SpoIIAA anti-anti-sigma activity.
About this Structure
1L0O is a Protein complex structure of sequences from Geobacillus stearothermophilus with and as ligands. Full crystallographic information is available from OCA.
Reference
Crystal structure of the Bacillus stearothermophilus anti-sigma factor SpoIIAB with the sporulation sigma factor sigmaF., Campbell EA, Masuda S, Sun JL, Muzzin O, Olson CA, Wang S, Darst SA, Cell. 2002 Mar 22;108(6):795-807. PMID:11955433
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