1srr
From Proteopedia
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|PDB= 1srr |SIZE=350|CAPTION= <scene name='initialview01'>1srr</scene>, resolution 1.9Å | |PDB= 1srr |SIZE=350|CAPTION= <scene name='initialview01'>1srr</scene>, resolution 1.9Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= SPO0F ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 Bacillus subtilis]) | |GENE= SPO0F ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 Bacillus subtilis]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1srr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1srr OCA], [http://www.ebi.ac.uk/pdbsum/1srr PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1srr RCSB]</span> | ||
}} | }} | ||
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[[Category: Xuong, N H.]] | [[Category: Xuong, N H.]] | ||
[[Category: Zapf, J.]] | [[Category: Zapf, J.]] | ||
| - | [[Category: CA]] | ||
[[Category: aspartate pocket]] | [[Category: aspartate pocket]] | ||
[[Category: regulatory protein]] | [[Category: regulatory protein]] | ||
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[[Category: two component system]] | [[Category: two component system]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:46:08 2008'' |
Revision as of 20:46, 30 March 2008
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| , resolution 1.9Å | |||||||
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| Ligands: | |||||||
| Gene: | SPO0F (Bacillus subtilis) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF A PHOSPHATASE RESISTANT MUTANT OF SPORULATION RESPONSE REGULATOR SPO0F FROM BACILLUS SUBTILIS
Overview
BACKGROUND: Spo0F, a phosphotransferase containing an aspartyl pocket, is involved in the signaling pathway (phosphorelay) controlling sporulation in Bacillus subtilis. It belongs to the superfamily of bacterial response regulatory proteins, which are activated upon phosphorylation of an invariant aspartate residue. This phosphorylation is carried out in a divalent cation dependent reaction catalyzed by cognate histidine kinases. Knowledge of the Spo0F structure would provide valuable information that would enable the elucidation of its function as a secondary messenger in a system in which a phosphate is donated from Spo0F to Spo0B, the third of four main proteins that constitute the phosphorelay. RESULTS: We have determined the crystal structure of a Rap phosphatase resistant mutant, Spo0F Tyr13-->Ser, at 1.9 A resolution. The structure was solved by single isomorphous replacement and anomalous scattering techniques. The overall structural fold is (beta/alpha)5 and contains a central beta sheet. The active site of the molecule is formed by three aspartate residues and a lysine residue which come together at the C terminus of the beta sheet. The active site accommodates a calcium ion. CONCLUSIONS: The structural analysis reveals that the overall topology and metal-binding coordination at the active site are similar to those of the bacterial chemotaxis response regulator CheY. Structural differences between Spo0F and CheY in the vicinity of the active site provide an insight into how similar molecular scaffolds can be adapted to perform different biological roles by the alteration of only a few amino acid residues. These differences may contribute to the observed stability of the phosphorylated species of Spo0F, a feature demanded by its role as a secondary messenger within the phosphorelay system which controls sporulation.
About this Structure
1SRR is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.
Reference
Crystal structure of a phosphatase-resistant mutant of sporulation response regulator Spo0F from Bacillus subtilis., Madhusudan, Zapf J, Whiteley JM, Hoch JA, Xuong NH, Varughese KI, Structure. 1996 Jun 15;4(6):679-90. PMID:8805550
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