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| - | [[Image:1h4x.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1h4x| PDB=1h4x | SCENE= }} | | {{STRUCTURE_1h4x| PDB=1h4x | SCENE= }} |
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| - | '''STRUCTURE OF THE BACILLUS CELL FATE DETERMINANT SPOIIAA IN THE PHOSPHORYLATED FORM'''
| + | ===STRUCTURE OF THE BACILLUS CELL FATE DETERMINANT SPOIIAA IN THE PHOSPHORYLATED FORM=== |
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| - | ==Overview==
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| - | BACKGROUND: The asymmetric cell division during sporulation in Bacillus subtilis gives rise to two compartments: the mother cell and the forespore. Each follow different programs of gene expression coordinated by a succession of alternate RNA polymerase sigma factors. The activity of the first of these sigma factors, sigmaF, is restricted to the forespore although sigmaF is present in the predivisional cell and partitions into both compartments following the asymmetric septation. For sigmaF to become active, it must escape from a complex with its cognate anti-sigma factor, SpoIIAB. This relief from SpoIIAB inhibition requires the dephosphorylation of the anti-sigma factor antagonist, SpoIIAA. The phosphorylation state of SpoIIAA is thus a key determinant of sigmaF activity and cell fate. RESULTS: We have solved the crystal structures of SpoIIAA from Bacillus sphaericus in its phosphorylated and unphosphorylated forms. The overall structure consists of a central beta-pleated sheet, one face of which is buried by a pair of alpha helices, while the other is largely exposed to solvent. The site of phosphorylation, Ser57, is located at the N terminus of helix alpha2. The phosphoserine is exceptionally well defined in the 1.2 A electron density maps, revealing that the structural changes accompanying phosphorylation are slight. CONCLUSIONS: Comparison of unphosphorylated and phosphorylated SpoIIAA shows that covalent modification has no significant effect on the global structure of the protein. The phosphoryl group has a passive role as a negatively charged flag rather than the active role it plays as a nucleus of structural reorganization in many eukaryotic signaling systems.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_11470435}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 11470435 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_11470435}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Sigma factor]] | | [[Category: Sigma factor]] |
| | [[Category: Sporulation]] | | [[Category: Sporulation]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 18:26:06 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 06:37:48 2008'' |
Revision as of 03:37, 1 July 2008
Template:STRUCTURE 1h4x
STRUCTURE OF THE BACILLUS CELL FATE DETERMINANT SPOIIAA IN THE PHOSPHORYLATED FORM
Template:ABSTRACT PUBMED 11470435
About this Structure
1H4X is a Single protein structure of sequence from Lysinibacillus sphaericus. Full crystallographic information is available from OCA.
Reference
Structure of the Bacillus cell fate determinant SpoIIAA in phosphorylated and unphosphorylated forms., Seavers PR, Lewis RJ, Brannigan JA, Verschueren KH, Murshudov GN, Wilkinson AJ, Structure. 2001 Jul 3;9(7):605-14. PMID:11470435
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