3ouv: Difference between revisions
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==SeMet Derivative of L512M mutant of PASTA domain 3 of Mycobacterium tuberculosis PknB== | ==SeMet Derivative of L512M mutant of PASTA domain 3 of Mycobacterium tuberculosis PknB== | ||
<StructureSection load='3ouv' size='340' side='right' caption='[[3ouv]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='3ouv' size='340' side='right'caption='[[3ouv]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3ouv]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3ouv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycta Mycta]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OUV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OUV FirstGlance]. <br> | ||
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pknB, MRA_0016 ([ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pknB, MRA_0016 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=419947 MYCTA])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3ouv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ouv OCA], [https://pdbe.org/3ouv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ouv RCSB], [https://www.ebi.ac.uk/pdbsum/3ouv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ouv ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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==See Also== | ==See Also== | ||
*[[Serine/threonine protein kinase|Serine/threonine protein kinase]] | *[[Serine/threonine protein kinase 3D structures|Serine/threonine protein kinase 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Mycta]] | [[Category: Mycta]] | ||
[[Category: Alber, T]] | [[Category: Alber, T]] | ||
Revision as of 13:58, 18 May 2022
SeMet Derivative of L512M mutant of PASTA domain 3 of Mycobacterium tuberculosis PknBSeMet Derivative of L512M mutant of PASTA domain 3 of Mycobacterium tuberculosis PknB
Structural highlights
Publication Abstract from PubMedMonitoring the environment with serine/threonine protein kinases is critical for growth and survival of Mycobacterium tuberculosis, a devastating human pathogen. Protein Kinase B (PknB) is a trans-membrane serine/threonine protein kinase that acts as an essential regulator of mycobacterial growth and division. The PknB extracellular domain (ECD) consists of four repeats homologous to penicillin-binding protein and serine/threonine kinase associated (PASTA) domains, and binds fragments of peptidoglycan. These properties suggest that PknB activity is modulated by ECD binding to peptidoglycan substructures, however the molecular mechanisms underpinning PknB regulation remain unclear. In this study, we report structural and genetic characterization of the PknB ECD. We determined the crystal structures of overlapping ECD fragments at near atomic resolution, built a model of the full ECD, and discovered a region on the C-terminal PASTA domain that has the properties of a ligand-binding site. Hydrophobic interaction between this surface and a bound molecule of citrate was observed in a crystal structure. Our genetic analyses in Mycobacterium tuberculosis showed that nonfunctional alleles were produced either by deletion of any of single PASTA domain or by mutation of individual conserved residues lining the putative ligand-binding surface of the C-terminal PASTA repeat. These results define two distinct structural features necessary for PknB signal transduction, a fully extended ECD and a conserved, membrane-distal putative ligand-binding site. Structural and genetic analyses of the Mycobacterium tuberculosis Protein Kinase B sensor domain identify a potential ligand binding site.,Prigozhin DM, Papavinasasundaram KG, Baer CE, Murphy KC, Moskaleva A, Chen TY, Alber T, Sassetti CM J Biol Chem. 2016 Sep 6. pii: jbc.M116.731760. PMID:27601474[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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