1kmi: Difference between revisions

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New page: left|200px<br /><applet load="1kmi" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kmi, resolution 2.9Å" /> '''CRYSTAL STRUCTURE OF ...
 
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[[Image:1kmi.gif|left|200px]]<br /><applet load="1kmi" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1kmi.gif|left|200px]]<br /><applet load="1kmi" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1kmi, resolution 2.9&Aring;" />
caption="1kmi, resolution 2.9&Aring;" />
'''CRYSTAL STRUCTURE OF AN E.COLI CHEMOTAXIS PROTEIN, CHEZ'''<br />
'''CRYSTAL STRUCTURE OF AN E.COLI CHEMOTAXIS PROTEIN, CHEZ'''<br />


==Overview==
==Overview==
The protein CheZ, which has the last unknown structure in the Escherichia, coli chemotaxis pathway, stimulates the dephosphorylation of the response, regulator CheY by an unknown mechanism. Here we report the co-crystal, structure of CheZ with CheY, Mg(2+) and the phosphoryl analog, BeF(3)(-)., The predominant structural feature of the CheZ dimer is a long four-helix, bundle composed of two helices from each monomer. The side chain of Gln, 147 of CheZ inserts into the CheY active site and is essential to the, dephosphorylation activity of CheZ. Gln 147 may orient a water molecule, for nucleophilic attack, similar to the role of the conserved Gln residue, in the RAS family of GTPases. Similarities between the CheY[bond] CheZ and, Spo0F [bond]Spo0B structures suggest a general mode of interaction for, modulation of response regulator phosphorylation chemistry.
The protein CheZ, which has the last unknown structure in the Escherichia coli chemotaxis pathway, stimulates the dephosphorylation of the response regulator CheY by an unknown mechanism. Here we report the co-crystal structure of CheZ with CheY, Mg(2+) and the phosphoryl analog, BeF(3)(-). The predominant structural feature of the CheZ dimer is a long four-helix bundle composed of two helices from each monomer. The side chain of Gln 147 of CheZ inserts into the CheY active site and is essential to the dephosphorylation activity of CheZ. Gln 147 may orient a water molecule for nucleophilic attack, similar to the role of the conserved Gln residue in the RAS family of GTPases. Similarities between the CheY[bond] CheZ and Spo0F [bond]Spo0B structures suggest a general mode of interaction for modulation of response regulator phosphorylation chemistry.


==About this Structure==
==About this Structure==
1KMI is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with MG, BEF and BCN as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1KMI OCA].  
1KMI is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=BEF:'>BEF</scene> and <scene name='pdbligand=BCN:'>BCN</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KMI OCA].  


==Reference==
==Reference==
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Bourret, R.B.]]
[[Category: Bourret, R B.]]
[[Category: Collins, E.J.]]
[[Category: Collins, E J.]]
[[Category: Silversmith, R.E.]]
[[Category: Silversmith, R E.]]
[[Category: Zhao, R.]]
[[Category: Zhao, R.]]
[[Category: BCN]]
[[Category: BCN]]
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[[Category: four-helix bundle]]
[[Category: four-helix bundle]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 19:22:08 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:35:44 2008''

Revision as of 14:35, 21 February 2008

File:1kmi.gif


1kmi, resolution 2.9Å

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CRYSTAL STRUCTURE OF AN E.COLI CHEMOTAXIS PROTEIN, CHEZ

OverviewOverview

The protein CheZ, which has the last unknown structure in the Escherichia coli chemotaxis pathway, stimulates the dephosphorylation of the response regulator CheY by an unknown mechanism. Here we report the co-crystal structure of CheZ with CheY, Mg(2+) and the phosphoryl analog, BeF(3)(-). The predominant structural feature of the CheZ dimer is a long four-helix bundle composed of two helices from each monomer. The side chain of Gln 147 of CheZ inserts into the CheY active site and is essential to the dephosphorylation activity of CheZ. Gln 147 may orient a water molecule for nucleophilic attack, similar to the role of the conserved Gln residue in the RAS family of GTPases. Similarities between the CheY[bond] CheZ and Spo0F [bond]Spo0B structures suggest a general mode of interaction for modulation of response regulator phosphorylation chemistry.

About this StructureAbout this Structure

1KMI is a Protein complex structure of sequences from Escherichia coli with , and as ligands. Full crystallographic information is available from OCA.

ReferenceReference

Structure and catalytic mechanism of the E. coli chemotaxis phosphatase CheZ., Zhao R, Collins EJ, Bourret RB, Silversmith RE, Nat Struct Biol. 2002 Aug;9(8):570-5. PMID:12080332

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