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3ke6
From Proteopedia
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| - | {{Seed}} | ||
| - | [[Image:3ke6.jpg|left|200px]] | ||
| - | + | ==The crystal structure of the RsbU and RsbW domains of Rv1364c from Mycobacterium tuberculosis== | |
| - | + | <StructureSection load='3ke6' size='340' side='right'caption='[[3ke6]], [[Resolution|resolution]] 2.60Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[3ke6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KE6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3KE6 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]] 2.6Å</td></tr> | |
| - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=3ke6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ke6 OCA], [https://pdbe.org/3ke6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ke6 RCSB], [https://www.ebi.ac.uk/pdbsum/3ke6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ke6 ProSAT]</span></td></tr> | |
| - | + | </table> | |
| - | + | == Function == | |
| - | + | [https://www.uniprot.org/uniprot/MTDRP_MYCTU MTDRP_MYCTU] Primarily acts as an independent SigF regulator that is sensitive to the osmosensory signal, mediating the cross talk of PknD with the SigF regulon (PubMed:30642988). Possesses both phosphatase and kinase activities (PubMed:30642988, PubMed:19700407). The kinase domain functions as a classic anti-sigma factor-like kinase to phosphorylate the anti-anti-sigma factor domain at the canonical regulatory site, and the phosphatase domain antagonizes this activity (PubMed:19700407).<ref>PMID:19700407</ref> <ref>PMID:30642988</ref> | |
| - | + | == References == | |
| - | == | + | <references/> |
| - | + | __TOC__ | |
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
[[Category: Mycobacterium tuberculosis]] | [[Category: Mycobacterium tuberculosis]] | ||
| - | [[Category: King-Scott | + | [[Category: King-Scott J]] |
| - | [[Category: Panjikar | + | [[Category: Panjikar S]] |
| - | [[Category: Tucker | + | [[Category: Tucker PA]] |
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Current revision
The crystal structure of the RsbU and RsbW domains of Rv1364c from Mycobacterium tuberculosis
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