1o6y

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[[Image:1o6y.gif|left|200px]]<br /><applet load="1o6y" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1o6y.gif|left|200px]]
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caption="1o6y, resolution 2.2&Aring;" />
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'''CATALYTIC DOMAIN OF PKNB KINASE FROM MYCOBACTERIUM TUBERCULOSIS'''<br />
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{{Structure
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|PDB= 1o6y |SIZE=350|CAPTION= <scene name='initialview01'>1o6y</scene>, resolution 2.2&Aring;
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|SITE= <scene name='pdbsite=ACP:Mg+Binding+Site+For+Chain+A'>ACP</scene>
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=ACP:PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER'>ACP</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Transferred_entry:_2.7.11.1 Transferred entry: 2.7.11.1], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.37 2.7.1.37]
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|GENE=
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}}
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'''CATALYTIC DOMAIN OF PKNB KINASE FROM MYCOBACTERIUM TUBERCULOSIS'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1O6Y 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=ACP:'>ACP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Transferred_entry:_2.7.11.1 Transferred entry: 2.7.11.1], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.37 2.7.1.37] Known structural/functional Site: <scene name='pdbsite=ACP:Mg+Binding+Site+For+Chain+A'>ACP</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O6Y OCA].
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1O6Y is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O6Y OCA].
==Reference==
==Reference==
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Crystal structure of the catalytic domain of the PknB serine/threonine kinase from Mycobacterium tuberculosis., Ortiz-Lombardia M, Pompeo F, Boitel B, Alzari PM, J Biol Chem. 2003 Apr 11;278(15):13094-100. Epub 2003 Jan 27. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12551895 12551895]
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Crystal structure of the catalytic domain of the PknB serine/threonine kinase from Mycobacterium tuberculosis., Ortiz-Lombardia M, Pompeo F, Boitel B, Alzari PM, J Biol Chem. 2003 Apr 11;278(15):13094-100. Epub 2003 Jan 27. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12551895 12551895]
[[Category: Mycobacterium tuberculosis]]
[[Category: Mycobacterium tuberculosis]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: transferase]]
[[Category: transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:14:06 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:06:37 2008''

Revision as of 11:06, 20 March 2008


PDB ID 1o6y

Drag the structure with the mouse to rotate
, resolution 2.2Å
Sites:
Ligands: and
Activity: Transferred entry: 2.7.11.1, with EC number 2.7.1.37
Coordinates: save as pdb, mmCIF, xml



CATALYTIC DOMAIN OF PKNB KINASE FROM MYCOBACTERIUM TUBERCULOSIS


Overview

With the advent of the sequencing programs of prokaryotic genomes, many examples of the presence of serine/threonine protein kinases in these organisms have been identified. Moreover, these kinases could be classified as homologues of those belonging to the well characterized superfamily of the eukaryotic serine/threonine and tyrosine kinases. Eleven such kinases were recognized in the genome of Mycobacterium tuberculosis. Here we report the crystal structure of an active form of PknB, one of the four M. tuberculosis kinases that are conserved in the downsized genome of Mycobacterium leprae and are therefore presumed to play an important role in the processes that regulate the complex life cycle of mycobacteria. Our structure confirms again the extraordinary conservation of the protein kinase fold and constitutes a landmark that extends this conservation across the evolutionary distance between high eukaryotes and eubacteria. The structure of PknB, in complex with a nucleotide triphosphate analog, reveals an enzyme in the active state with an unprecedented arrangement of the Gly-rich loop associated with a new conformation of the nucleotide gamma-phosphoryl group. It presents as well a partially disordered activation loop, suggesting an induced fit mode of binding for the so far unknown substrates of this kinase or for some modulating factor(s).

About this Structure

1O6Y is a Single protein structure of sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA.

Reference

Crystal structure of the catalytic domain of the PknB serine/threonine kinase from Mycobacterium tuberculosis., Ortiz-Lombardia M, Pompeo F, Boitel B, Alzari PM, J Biol Chem. 2003 Apr 11;278(15):13094-100. Epub 2003 Jan 27. PMID:12551895

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