1dz3

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[[Image:1dz3.jpg|left|200px]]
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{{Structure
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|PDB= 1dz3 |SIZE=350|CAPTION= <scene name='initialview01'>1dz3</scene>, resolution 1.65&Aring;
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The line below this paragraph, containing "STRUCTURE_1dz3", creates the "Structure Box" on the page.
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|GENE= SPO0A ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1422 Geobacillus stearothermophilus])
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dz3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dz3 OCA], [http://www.ebi.ac.uk/pdbsum/1dz3 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1dz3 RCSB]</span>
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'''DOMAIN-SWAPPING IN THE SPORULATION RESPONSE REGULATOR SPO0A'''
'''DOMAIN-SWAPPING IN THE SPORULATION RESPONSE REGULATOR SPO0A'''
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[[Category: Muchova, K.]]
[[Category: Muchova, K.]]
[[Category: Wilkinson, A J.]]
[[Category: Wilkinson, A J.]]
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[[Category: domain swapping]]
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[[Category: Domain swapping]]
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[[Category: response regulator]]
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[[Category: Response regulator]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:27:21 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:51:38 2008''
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Revision as of 11:27, 2 May 2008

Template:STRUCTURE 1dz3

DOMAIN-SWAPPING IN THE SPORULATION RESPONSE REGULATOR SPO0A


Overview

Adaptive responses of micro-organisms, such as chemotaxis and sporulation, are governed by two-component systems consisting of sensor kinases, that interpret environmental signals, and response regulators which activate the appropriate physiological responses. Signal transduction via response regulator proteins is mediated through transient phosphorylation of aspartic acid residues. In Spo0A, the key regulator of development (sporulation) in Bacillus, phosphorylation of the N-terminal receiver domain (N-Spo0A) at aspartate-55 switches on the transcription activation functions residing in the C-terminal effector domain. Here we report the crystal structure of N-Spo0A from Bacillus stearothermophilus at 1.6 A spacing, revealing a dimer formed by an alpha-helix swap. Comparison of this structure with the recently described structure of phosphorylated N-Spo0A shows that dimer formation results from a cis-trans isomerization of the Lys106--Pro107 peptide bond. The quaternary reorganization is associated with alterations in the active site stereochemistry which may have implications for signalling. Remarkably, this 3-D domain swapped N-Spo0A dimer has an identical topology to a hypothetical CheY-like dimer, recently proposed as an intermediate in the evolution of the family of periplasmic substrate binding proteins.

About this Structure

1DZ3 is a Single protein structure of sequence from Geobacillus stearothermophilus. Full crystallographic information is available from OCA.

Reference

Domain swapping in the sporulation response regulator Spo0A., Lewis RJ, Muchova K, Brannigan JA, Barak I, Leonard G, Wilkinson AJ, J Mol Biol. 2000 Mar 31;297(3):757-70. PMID:10731426 Page seeded by OCA on Fri May 2 14:27:21 2008

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