1b0n
From Proteopedia
(New page: 200px<br /><applet load="1b0n" size="450" color="white" frame="true" align="right" spinBox="true" caption="1b0n, resolution 1.90Å" /> '''SINR PROTEIN/SINI PR...) |
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| - | [[Image:1b0n.jpg|left|200px]]<br /><applet load="1b0n" size=" | + | [[Image:1b0n.jpg|left|200px]]<br /><applet load="1b0n" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1b0n, resolution 1.90Å" /> | caption="1b0n, resolution 1.90Å" /> | ||
'''SINR PROTEIN/SINI PROTEIN COMPLEX'''<br /> | '''SINR PROTEIN/SINI PROTEIN COMPLEX'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Spore formation is an extreme response of some bacteria to adversity. In | + | Spore formation is an extreme response of some bacteria to adversity. In Bacillus subtilis the proteins of the sin, sporulation inhibition, region form a component of an elaborate molecular circuitry that regulates the commitment to sporulation. SinR is a tetrameric repressor protein that binds to the promoters of genes essential for entry into sporulation and prevents their transcription. This repression is overcome through the activity of SinI, which disrupts the SinR tetramer through the formation of a SinI-SinR heterodimer. The interactions governing this curious quaternary transition are revealed in the crystal structure of the SinI-SinR complex. The most striking, and unexpected, finding is that the tertiary structure of the DNA-binding domain of SinR is identical with that of the corresponding domains of the repressor proteins, CI and Cro, of bacteriophage 434 that regulate lysis/lysogeny. This structural similarity greatly exceeds that between SinR and any bacterial protein or between the 434 repressor proteins and their homologues in the closely related bacteriophage lambda. The close evolutionary relationship implied by the structures of SinR and the 434 repressors provokes both comparison of their functions and a speculative consideration of the intriguing possibility of an evolutionary link between the two adaptive responses, sporulation and prophage induction. |
==About this Structure== | ==About this Structure== | ||
| - | 1B0N is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1B0N is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B0N OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Bacillus subtilis]] | [[Category: Bacillus subtilis]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Brannigan, J | + | [[Category: Brannigan, J A.]] |
| - | [[Category: Lewis, R | + | [[Category: Lewis, R J.]] |
| - | [[Category: Offen, W | + | [[Category: Offen, W A.]] |
[[Category: Smith, I.]] | [[Category: Smith, I.]] | ||
| - | [[Category: Wilkinson, A | + | [[Category: Wilkinson, A J.]] |
[[Category: ZN]] | [[Category: ZN]] | ||
[[Category: antagonist]] | [[Category: antagonist]] | ||
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[[Category: transcription regulator]] | [[Category: transcription regulator]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:50:16 2008'' |
Revision as of 09:50, 21 February 2008
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SINR PROTEIN/SINI PROTEIN COMPLEX
Overview
Spore formation is an extreme response of some bacteria to adversity. In Bacillus subtilis the proteins of the sin, sporulation inhibition, region form a component of an elaborate molecular circuitry that regulates the commitment to sporulation. SinR is a tetrameric repressor protein that binds to the promoters of genes essential for entry into sporulation and prevents their transcription. This repression is overcome through the activity of SinI, which disrupts the SinR tetramer through the formation of a SinI-SinR heterodimer. The interactions governing this curious quaternary transition are revealed in the crystal structure of the SinI-SinR complex. The most striking, and unexpected, finding is that the tertiary structure of the DNA-binding domain of SinR is identical with that of the corresponding domains of the repressor proteins, CI and Cro, of bacteriophage 434 that regulate lysis/lysogeny. This structural similarity greatly exceeds that between SinR and any bacterial protein or between the 434 repressor proteins and their homologues in the closely related bacteriophage lambda. The close evolutionary relationship implied by the structures of SinR and the 434 repressors provokes both comparison of their functions and a speculative consideration of the intriguing possibility of an evolutionary link between the two adaptive responses, sporulation and prophage induction.
About this Structure
1B0N is a Protein complex structure of sequences from Bacillus subtilis with as ligand. Full crystallographic information is available from OCA.
Reference
An evolutionary link between sporulation and prophage induction in the structure of a repressor:anti-repressor complex., Lewis RJ, Brannigan JA, Offen WA, Smith I, Wilkinson AJ, J Mol Biol. 1998 Nov 13;283(5):907-12. PMID:9799632
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