1ixm: Difference between revisions

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New page: left|200px<br /><applet load="1ixm" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ixm, resolution 2.6Å" /> '''CRYSTAL STRUCTURE OF ...
 
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[[Image:1ixm.gif|left|200px]]<br /><applet load="1ixm" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1ixm.gif|left|200px]]<br /><applet load="1ixm" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1ixm, resolution 2.6&Aring;" />
caption="1ixm, resolution 2.6&Aring;" />
'''CRYSTAL STRUCTURE OF SPOOB FROM BACILLUS SUBTILIS'''<br />
'''CRYSTAL STRUCTURE OF SPOOB FROM BACILLUS SUBTILIS'''<br />


==Overview==
==Overview==
A basis for understanding specificity of molecular recognition between, phosphorelay proteins has been deduced from the 2.6 A structure of the, Spo0B phosphotransferase of the phosphorelay regulating sporulation, initiation. Spo0B consists of two domains: an N-terminal alpha-helical, hairpin domain and a C-terminal alpha/beta domain. Two subunits of Spo0B, dimerize by a parallel association of helical hairpins to form a novel, four-helix bundle from which the active histidine protrudes. Docking, studies show that both the monomers interact with a Spo0F molecule at the, region surrounding the active site aspartate to position it for, phosphotransfer. It is apparent that different surfaces of response, regulators may be involved in recognition of the protein partners to which, they are paired.
A basis for understanding specificity of molecular recognition between phosphorelay proteins has been deduced from the 2.6 A structure of the Spo0B phosphotransferase of the phosphorelay regulating sporulation initiation. Spo0B consists of two domains: an N-terminal alpha-helical hairpin domain and a C-terminal alpha/beta domain. Two subunits of Spo0B dimerize by a parallel association of helical hairpins to form a novel four-helix bundle from which the active histidine protrudes. Docking studies show that both the monomers interact with a Spo0F molecule at the region surrounding the active site aspartate to position it for phosphotransfer. It is apparent that different surfaces of response regulators may be involved in recognition of the protein partners to which they are paired.


==About this Structure==
==About this Structure==
1IXM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1IXM OCA].  
1IXM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IXM OCA].  


==Reference==
==Reference==
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[[Category: Bacillus subtilis]]
[[Category: Bacillus subtilis]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Varughese, K.I.]]
[[Category: Varughese, K I.]]
[[Category: phosphotransferase]]
[[Category: phosphotransferase]]
[[Category: regulatory protein]]
[[Category: regulatory protein]]
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[[Category: two component system]]
[[Category: two component system]]


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Revision as of 14:16, 21 February 2008

File:1ixm.gif


1ixm, resolution 2.6Å

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CRYSTAL STRUCTURE OF SPOOB FROM BACILLUS SUBTILIS

OverviewOverview

A basis for understanding specificity of molecular recognition between phosphorelay proteins has been deduced from the 2.6 A structure of the Spo0B phosphotransferase of the phosphorelay regulating sporulation initiation. Spo0B consists of two domains: an N-terminal alpha-helical hairpin domain and a C-terminal alpha/beta domain. Two subunits of Spo0B dimerize by a parallel association of helical hairpins to form a novel four-helix bundle from which the active histidine protrudes. Docking studies show that both the monomers interact with a Spo0F molecule at the region surrounding the active site aspartate to position it for phosphotransfer. It is apparent that different surfaces of response regulators may be involved in recognition of the protein partners to which they are paired.

About this StructureAbout this Structure

1IXM is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.

ReferenceReference

Formation of a novel four-helix bundle and molecular recognition sites by dimerization of a response regulator phosphotransferase., Varughese KI, Madhusudan, Zhou XZ, Whiteley JM, Hoch JA, Mol Cell. 1998 Oct;2(4):485-93. PMID:9809070

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