1o6y
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:1o6y.gif|left|200px]] | [[Image:1o6y.gif|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_1o6y", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | + | or leave the SCENE parameter empty for the default display. | |
| - | | | + | --> |
| - | | | + | {{STRUCTURE_1o6y| PDB=1o6y | SCENE= }} |
| - | + | ||
| - | + | ||
| - | }} | + | |
'''CATALYTIC DOMAIN OF PKNB KINASE FROM MYCOBACTERIUM TUBERCULOSIS''' | '''CATALYTIC DOMAIN OF PKNB KINASE FROM MYCOBACTERIUM TUBERCULOSIS''' | ||
| Line 31: | Line 28: | ||
[[Category: Pompeo, F.]] | [[Category: Pompeo, F.]] | ||
[[Category: TBSGC, TB Structural Genomics Consortium.]] | [[Category: TBSGC, TB Structural Genomics Consortium.]] | ||
| - | [[Category: | + | [[Category: Serine/threonine protein kinase]] |
| - | [[Category: | + | [[Category: Tbsgc]] |
| - | [[Category: | + | [[Category: Transferase,psi,protein structure initiative,tb structural genomics consortium,tb]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 03:27:36 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 00:27, 3 May 2008
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 Page seeded by OCA on Sat May 3 03:27:36 2008
Categories: Mycobacterium tuberculosis | Non-specific serine/threonine protein kinase | Single protein | Alzari, P M. | Boitel, B. | Ortiz-Lombardia, M. | Pompeo, F. | TBSGC, TB Structural Genomics Consortium. | Serine/threonine protein kinase | Tbsgc | Transferase,psi,protein structure initiative,tb structural genomics consortium,tb
