3ouv: Difference between revisions

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-[[Image:3ouv.png|left|200px]]
-{{STRUCTURE_3ouv|  PDB=3ouv  |  SCENE=  }}
+==SeMet Derivative of L512M mutant of PASTA domain 3 of Mycobacterium tuberculosis PknB==
+<StructureSection load='3ouv' size='340' side='right'caption='[[3ouv]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[3ouv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_H37Ra Mycobacterium tuberculosis H37Ra]. 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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.004&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
+<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>
+== Function ==
+[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>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Monitoring 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.
-===SeMet Derivative of L512M mutant of PASTA domain 3 of Mycobacterium tuberculosis PknB===
+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<ref>PMID:27601474</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-==About this Structure==
+</div>
-[[3ouv]] is a 1 chain structure of [[Serine/threonine protein kinase]] with sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_h37ra Mycobacterium tuberculosis h37ra]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OUV OCA].
+<div class="pdbe-citations 3ouv" style="background-color:#fffaf0;"></div>
 ==See Also==
-*[[Serine/threonine protein kinase|Serine/threonine protein kinase]]
+*[[Serine/threonine protein kinase 3D structures|Serine/threonine protein kinase 3D structures]]
-[[Category: Mycobacterium tuberculosis h37ra]]
+== References ==
-[[Category: Alber, T.]]
+<references/>
-[[Category: Chen, T Y.]]
+__TOC__
-[[Category: Prigozhin, D M.]]
+</StructureSection>
-[[Category: Protein-ligand interaction]]
+[[Category: Large Structures]]
-[[Category: Transferase]]
+[[Category: Mycobacterium tuberculosis H37Ra]]
+[[Category: Alber T]]
+[[Category: Chen TY]]
+[[Category: Prigozhin DM]]