1o6y

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[[Image:1o6y.gif|left|200px]]
 
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{{Structure
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==Catalytic domain of PknB kinase from Mycobacterium tuberculosis==
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|PDB= 1o6y |SIZE=350|CAPTION= <scene name='initialview01'>1o6y</scene>, resolution 2.2&Aring;
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<StructureSection load='1o6y' size='340' side='right'caption='[[1o6y]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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|SITE= <scene name='pdbsite=ACP:Mg+Binding+Site+For+Chain+A'>ACP</scene>
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=ACP:PHOSPHOMETHYLPHOSPHONIC+ACID+ADENYLATE+ESTER'>ACP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>
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<table><tr><td colspan='2'>[[1o6y]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_H37Rv Mycobacterium tuberculosis H37Rv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O6Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1O6Y FirstGlance]. <br>
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|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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACP:PHOSPHOMETHYLPHOSPHONIC+ACID+ADENYLATE+ESTER'>ACP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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|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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1o6y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o6y OCA], [https://pdbe.org/1o6y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1o6y RCSB], [https://www.ebi.ac.uk/pdbsum/1o6y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1o6y ProSAT], [https://www.topsan.org/Proteins/TBSGC/1o6y TOPSAN]</span></td></tr>
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|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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</table>
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}}
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== Function ==
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[https://www.uniprot.org/uniprot/PKNB_MYCTU PKNB_MYCTU] Key component of a signal transduction pathway that regulates cell growth and cell division via phosphorylation of target proteins such as GarA, GlmU, PapA5, PbpA, FhaB (Rv0019c), FhaA (Rv0020c), MviN, PstP, EmbR, Rv1422, Rv1747 and RseA. Shows a strong preference for Thr versus Ser as the phosphoacceptor.<ref>PMID:15985609</ref> <ref>PMID:15978616</ref> <ref>PMID:15987910</ref> <ref>PMID:16817899</ref> <ref>PMID:16980473</ref> <ref>PMID:16436437</ref> <ref>PMID:19826007</ref> <ref>PMID:19121323</ref> <ref>PMID:20025669</ref> <ref>PMID:21423706</ref> <ref>PMID:22275220</ref>
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'''CATALYTIC DOMAIN OF PKNB KINASE FROM MYCOBACTERIUM TUBERCULOSIS'''
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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==Overview==
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/o6/1o6y_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1o6y ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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).
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).
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==About this Structure==
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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:12551895<ref>PMID:12551895</ref>
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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].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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]
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</div>
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[[Category: Mycobacterium tuberculosis]]
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<div class="pdbe-citations 1o6y" style="background-color:#fffaf0;"></div>
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[[Category: Non-specific serine/threonine protein kinase]]
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[[Category: Single protein]]
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[[Category: Alzari, P M.]]
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[[Category: Boitel, B.]]
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[[Category: Ortiz-Lombardia, M.]]
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[[Category: Pompeo, F.]]
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[[Category: TBSGC, TB Structural Genomics Consortium.]]
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[[Category: serine/threonine protein kinase]]
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[[Category: tbsgc]]
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[[Category: transferase,psi,protein structure initiative,tb structural genomics consortium,tb]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Mar 26 05:59:42 2008''
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==See Also==
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*[[Serine/threonine protein kinase 3D structures|Serine/threonine protein kinase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Mycobacterium tuberculosis H37Rv]]
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[[Category: Alzari PM]]
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[[Category: Boitel B]]
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[[Category: Ortiz-Lombardia M]]
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[[Category: Pompeo F]]

Current revision

Catalytic domain of PknB kinase from Mycobacterium tuberculosis

PDB ID 1o6y

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