3orm: Difference between revisions
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<StructureSection load='3orm' size='340' side='right'caption='[[3orm]], [[Resolution|resolution]] 2.50Å' scene=''> | <StructureSection load='3orm' size='340' side='right'caption='[[3orm]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3orm]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[3orm]] 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=3ORM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ORM FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AGS:PHOSPHOTHIOPHOSPHORIC+ACID-ADENYLATE+ESTER'>AGS</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</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=3orm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3orm OCA], [https://pdbe.org/3orm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3orm RCSB], [https://www.ebi.ac.uk/pdbsum/3orm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3orm ProSAT]</span></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=3orm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3orm OCA], [https://pdbe.org/3orm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3orm RCSB], [https://www.ebi.ac.uk/pdbsum/3orm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3orm ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/A5TY84_MYCTA A5TY84_MYCTA] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Mycobacterium tuberculosis H37Ra]] | ||
[[Category: Alber | [[Category: Alber T]] | ||
[[Category: Echols | [[Category: Echols N]] | ||
[[Category: Lombana | [[Category: Lombana TN]] | ||
Latest revision as of 12:43, 6 September 2023
Mycobacterium tuberculosis PknB kinase domain D76A mutantMycobacterium tuberculosis PknB kinase domain D76A mutant
Structural highlights
FunctionPublication Abstract from PubMedThe essential Mycobacterium tuberculosis Ser/Thr protein kinase (STPK), PknB, plays a key role in regulating growth and division, but the structural basis of activation has not been defined. Here, we provide biochemical and structural evidence that dimerization through the kinase-domain (KD) N-lobe activates PknB by an allosteric mechanism. Promoting KD pairing using a small-molecule dimerizer stimulates the unphosphorylated kinase, and substitutions that disrupt N-lobe pairing decrease phosphorylation activity in vitro and in vivo. Multiple crystal structures of two monomeric PknB KD mutants in complex with nucleotide reveal diverse inactive conformations that contain large active-site distortions that propagate > 30 A from the mutation site. These results define flexible, inactive structures of a monomeric bacterial receptor KD and show how "back-to-back" N-lobe dimerization stabilizes the active KD conformation. This general mechanism of bacterial receptor STPK activation affords insights into the regulation of homologous eukaryotic kinases that form structurally similar dimers. Allosteric activation mechanism of the Mycobacterium tuberculosis receptor Ser/Thr protein kinase, PknB.,Lombana TN, Echols N, Good MC, Thomsen ND, Ng HL, Greenstein AE, Falick AM, King DS, Alber T Structure. 2010 Dec 8;18(12):1667-77. doi: 10.1016/j.str.2010.09.019. PMID:21134645[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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