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1mru

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(New page: 200px<br /><applet load="1mru" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mru, resolution 3.00&Aring;" /> '''Intracellular Ser/Th...)
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caption="1mru, resolution 3.00&Aring;" />
'''Intracellular Ser/Thr protein kinase domain of Mycobacterium tuberculosis PknB.'''<br />
'''Intracellular Ser/Thr protein kinase domain of Mycobacterium tuberculosis PknB.'''<br />
==Overview==
==Overview==
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A family of eukaryotic-like Ser/Thr protein kinases occurs in bacteria, but little is known about the structures and functions of these proteins., Here we characterize PknB, a transmembrane signaling kinase from, Mycobacterium tuberculosis. The intracellular PknB kinase domain is active, autonomously, and the active enzyme is phosphorylated on residues, homologous to regulatory phospho-acceptors in eukaryotic Ser/Thr kinases., The crystal structure of the PknB kinase domain in complex with an ATP, analog reveals the active conformation. The predicted fold of the PknB, extracellular domain matches the proposed targeting domain of, penicillin-binding protein 2x. The structural and chemical similarities of, PknB to metazoan homologs support a universal activation mechanism of, Ser/Thr protein kinases in prokaryotes and eukaryotes.
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A family of eukaryotic-like Ser/Thr protein kinases occurs in bacteria, but little is known about the structures and functions of these proteins. Here we characterize PknB, a transmembrane signaling kinase from Mycobacterium tuberculosis. The intracellular PknB kinase domain is active autonomously, and the active enzyme is phosphorylated on residues homologous to regulatory phospho-acceptors in eukaryotic Ser/Thr kinases. The crystal structure of the PknB kinase domain in complex with an ATP analog reveals the active conformation. The predicted fold of the PknB extracellular domain matches the proposed targeting domain of penicillin-binding protein 2x. The structural and chemical similarities of PknB to metazoan homologs support a universal activation mechanism of Ser/Thr protein kinases in prokaryotes and eukaryotes.
==About this Structure==
==About this Structure==
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1MRU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis] with MG and AGS as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1MRU OCA].
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1MRU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=AGS:'>AGS</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MRU OCA].
==Reference==
==Reference==
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[[Category: Alber, T.]]
[[Category: Alber, T.]]
[[Category: Delagoutte, B.]]
[[Category: Delagoutte, B.]]
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[[Category: Endrizzi, J.A.]]
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[[Category: Endrizzi, J A.]]
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[[Category: TBSGC, TB.Structural.Genomics.Consortium.]]
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[[Category: TBSGC, TB Structural Genomics Consortium.]]
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[[Category: Young, T.A.]]
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[[Category: Young, T A.]]
[[Category: AGS]]
[[Category: AGS]]
[[Category: MG]]
[[Category: MG]]
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[[Category: tbsgc]]
[[Category: tbsgc]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:39:42 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:58:24 2008''

Revision as of 11:58, 21 February 2008

Image:1mru.gif

1mru, resolution 3.00Å

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Intracellular Ser/Thr protein kinase domain of Mycobacterium tuberculosis PknB.

Overview

A family of eukaryotic-like Ser/Thr protein kinases occurs in bacteria, but little is known about the structures and functions of these proteins. Here we characterize PknB, a transmembrane signaling kinase from Mycobacterium tuberculosis. The intracellular PknB kinase domain is active autonomously, and the active enzyme is phosphorylated on residues homologous to regulatory phospho-acceptors in eukaryotic Ser/Thr kinases. The crystal structure of the PknB kinase domain in complex with an ATP analog reveals the active conformation. The predicted fold of the PknB extracellular domain matches the proposed targeting domain of penicillin-binding protein 2x. The structural and chemical similarities of PknB to metazoan homologs support a universal activation mechanism of Ser/Thr protein kinases in prokaryotes and eukaryotes.

About this Structure

1MRU is a Single protein structure of sequence from Mycobacterium tuberculosis with and as ligands. Full crystallographic information is available from OCA.

Reference

Structure of Mycobacterium tuberculosis PknB supports a universal activation mechanism for Ser/Thr protein kinases., Young TA, Delagoutte B, Endrizzi JA, Falick AM, Alber T, Nat Struct Biol. 2003 Mar;10(3):168-74. PMID:12548283

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