1l0o

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[[Image:1l0o.gif|left|200px]]<br /><applet load="1l0o" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1l0o.gif|left|200px]]
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caption="1l0o, resolution 2.9&Aring;" />
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'''Crystal Structure of the Bacillus stearothermophilus Anti-Sigma Factor SpoIIAB with the Sporulation Sigma Factor SigmaF'''<br />
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{{Structure
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|PDB= 1l0o |SIZE=350|CAPTION= <scene name='initialview01'>1l0o</scene>, resolution 2.9&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=ADP:ADENOSINE-5'-DIPHOSPHATE'>ADP</scene>
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|ACTIVITY=
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|GENE= SpoIIAB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1422 Geobacillus stearothermophilus])
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}}
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'''Crystal Structure of the Bacillus stearothermophilus Anti-Sigma Factor SpoIIAB with the Sporulation Sigma Factor SigmaF'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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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].
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1L0O is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L0O OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11955433 11955433]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/11955433 11955433]
[[Category: Geobacillus stearothermophilus]]
[[Category: Geobacillus stearothermophilus]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: helix-turn-helix]]
[[Category: helix-turn-helix]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:40:00 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:24:43 2008''

Revision as of 10:24, 20 March 2008


PDB ID 1l0o

Drag the structure with the mouse to rotate
, resolution 2.9Å
Ligands: and
Gene: SpoIIAB (Geobacillus stearothermophilus)
Coordinates: save as pdb, mmCIF, xml



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. 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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