1o6y
From Proteopedia
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|PDB= 1o6y |SIZE=350|CAPTION= <scene name='initialview01'>1o6y</scene>, resolution 2.2Å | |PDB= 1o6y |SIZE=350|CAPTION= <scene name='initialview01'>1o6y</scene>, resolution 2.2Å | ||
|SITE= <scene name='pdbsite=ACP:Mg+Binding+Site+For+Chain+A'>ACP</scene> | |SITE= <scene name='pdbsite=ACP:Mg+Binding+Site+For+Chain+A'>ACP</scene> | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=ACP:PHOSPHOMETHYLPHOSPHONIC+ACID+ADENYLATE+ESTER'>ACP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/ | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN=<span class='plainlinks'>[http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=cd00180 S_TKc], [http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=smart00220 S_TKc]</span> | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1o6y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o6y OCA], [http://www.ebi.ac.uk/pdbsum/1o6y PDBsum], [http://www.fli-leibniz.de/cgi-bin/ImgLib.pl?CODE=1kfv JenaLib], [http://www.rcsb.org/pdb/explore.do?structureId=1o6y RCSB]</span> | ||
}} | }} | ||
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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] | 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: Non-specific serine/threonine protein kinase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Transferred entry: 2 7.11 1]] | ||
[[Category: Alzari, P M.]] | [[Category: Alzari, P M.]] | ||
[[Category: Boitel, B.]] | [[Category: Boitel, B.]] | ||
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[[Category: Pompeo, F.]] | [[Category: Pompeo, F.]] | ||
[[Category: TBSGC, TB Structural Genomics Consortium.]] | [[Category: TBSGC, TB Structural Genomics Consortium.]] | ||
| - | [[Category: ACP]] | ||
| - | [[Category: MG]] | ||
| - | [[Category: protein structure initiative]] | ||
| - | [[Category: psi]] | ||
[[Category: serine/threonine protein kinase]] | [[Category: serine/threonine protein kinase]] | ||
| - | [[Category: tb]] | ||
| - | [[Category: tb structural genomics consortium]] | ||
[[Category: tbsgc]] | [[Category: tbsgc]] | ||
| - | [[Category: transferase]] | + | [[Category: transferase,psi,protein structure initiative,tb structural genomics consortium,tb]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Mar 26 05:59:42 2008'' |
Revision as of 03:59, 26 March 2008
| |||||||
| , resolution 2.2Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , | ||||||
| Activity: | Non-specific serine/threonine protein kinase, with EC number 2.7.11.1 | ||||||
| Domains: | S_TKc, S_TKc | ||||||
| Resources: | FirstGlance, OCA, PDBsum, JenaLib, RCSB | ||||||
| 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
Page seeded by OCA on Wed Mar 26 05:59:42 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
