1o6y
From Proteopedia
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==Overview== | ==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 .. | + | 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== | ==About this Structure== | ||
| - | 1O6Y is a | + | 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 MG and ACP 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] Structure known Active Site: ACP. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1O6Y OCA]. |
==Reference== | ==Reference== | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 12:50:42 2007'' |
Revision as of 10:45, 5 November 2007
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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 with MG and ACP as ligands. Active as Transferred entry: 2.7.11.1, with EC number 2.7.1.37 Structure known Active Site: ACP. 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 Mon Nov 5 12:50:42 2007
Categories: Mycobacterium tuberculosis | Single protein | Transferred entry: 2.7.11.1 | Alzari, P.M. | Boitel, B. | Ortiz-Lombardia, M. | Pompeo, F. | TBSGC, TB.Structural.Genomics.Consortium. | ACP | MG | Protein structure initiative | Psi | Serine/threonine protein kinase | Tb | Tb structural genomics consortium | Tbsgc | Transferase
