1b3q: Difference between revisions

Revision as of 12:51, 21 February 2008

CRYSTAL STRUCTURE OF CHEA-289, A SIGNAL TRANSDUCING HISTIDINE KINASE

OverviewOverview

Histidine kinases allow bacteria, plants, and fungi to sense and respond to their environment. The 2.6 A resolution crystal structure of Thermotoga maritima CheA (290-671) histidine kinase reveals a dimer where the functions of dimerization, ATP binding, and regulation are segregated into domains. The kinase domain is unlike Ser/Thr/Tyr kinases but resembles two ATPases, Gyrase B and Hsp90. Structural analogies within this superfamily suggest that the P1 domain of CheA provides the nucleophilic histidine and activating glutamate for phosphotransfer. The regulatory domain, which binds the homologous receptor-coupling protein CheW, topologically resembles two SH3 domains and provides different protein recognition surfaces at each end. The dimerization domain forms a central four-helix bundle about which the kinase and regulatory domains pivot on conserved hinges to modulate transphosphorylation. Different subunit conformations suggest that relative domain motions link receptor response to kinase activity.

About this StructureAbout this Structure

1B3Q is a Single protein structure of sequence from Thermotoga maritima with as ligand. Full crystallographic information is available from OCA.

ReferenceReference

Structure of CheA, a signal-transducing histidine kinase., Bilwes AM, Alex LA, Crane BR, Simon MI, Cell. 1999 Jan 8;96(1):131-41. PMID:9989504

Page seeded by OCA on Thu Feb 21 11:51:06 2008

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OCA

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-[[Image:1b3q.gif|left|200px]]<br /><applet load="1b3q" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1b3q.gif|left|200px]]<br /><applet load="1b3q" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1b3q, resolution 2.6&Aring;" />
 '''CRYSTAL STRUCTURE OF CHEA-289, A SIGNAL TRANSDUCING HISTIDINE KINASE'''<br />
 ==Overview==
-Histidine kinases allow bacteria, plants, and fungi to sense and respond, to their environment. The 2.6 A resolution crystal structure of Thermotoga, maritima CheA (290-671) histidine kinase reveals a dimer where the, functions of dimerization, ATP binding, and regulation are segregated into, domains. The kinase domain is unlike Ser/Thr/Tyr kinases but resembles two, ATPases, Gyrase B and Hsp90. Structural analogies within this superfamily, suggest that the P1 domain of CheA provides the nucleophilic histidine and, activating glutamate for phosphotransfer. The regulatory domain, which, binds the homologous receptor-coupling protein CheW, topologically, resembles two SH3 domains and provides different protein recognition, surfaces at each end. The dimerization domain forms a central four-helix, bundle about which the kinase and regulatory domains pivot on conserved, hinges to modulate transphosphorylation. Different subunit conformations, suggest that relative domain motions link receptor response to kinase, activity.
+Histidine kinases allow bacteria, plants, and fungi to sense and respond to their environment. The 2.6 A resolution crystal structure of Thermotoga maritima CheA (290-671) histidine kinase reveals a dimer where the functions of dimerization, ATP binding, and regulation are segregated into domains. The kinase domain is unlike Ser/Thr/Tyr kinases but resembles two ATPases, Gyrase B and Hsp90. Structural analogies within this superfamily suggest that the P1 domain of CheA provides the nucleophilic histidine and activating glutamate for phosphotransfer. The regulatory domain, which binds the homologous receptor-coupling protein CheW, topologically resembles two SH3 domains and provides different protein recognition surfaces at each end. The dimerization domain forms a central four-helix bundle about which the kinase and regulatory domains pivot on conserved hinges to modulate transphosphorylation. Different subunit conformations suggest that relative domain motions link receptor response to kinase activity.
 ==About this Structure==
-B3Q is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima] with HG as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1B3Q OCA].
+B3Q is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima] with <scene name='pdbligand=HG:'>HG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B3Q OCA].
 ==Reference==
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 [[Category: Single protein]]
 [[Category: Thermotoga maritima]]
-[[Category: Alex, L.A.]]
+[[Category: Alex, L A.]]
-[[Category: Bilwes, A.M.]]
+[[Category: Bilwes, A M.]]
-[[Category: Crane, B.R.]]
+[[Category: Crane, B R.]]
-[[Category: Simon, M.I.]]
+[[Category: Simon, M I.]]
 [[Category: HG]]
 [[Category: chemotaxis]]
@@ Line 23: / Line 23: @@
 [[Category: signal transduction]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 11:19:48 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:51:06 2008''