2KFU
PknB-phosphorylated Rv1827
Summary for 2KFU
| Entry DOI | 10.2210/pdb2kfu/pdb |
| NMR Information | BMRB: 16248 |
| Descriptor | Rv1827 pThr 22 (1 entity in total) |
| Functional Keywords | fha domain, mycobacterium tuberculosis, phosphorylation, intramolecular interaction, glutamate metabolism, phosphoprotein, protein binding |
| Biological source | Mycobacterium tuberculosis |
| Total number of polymer chains | 1 |
| Total formula weight | 17313.74 |
| Authors | Smerdon, S.J.,Nott, T.J.,Kelly, G. (deposition date: 2009-02-27, release date: 2009-06-16, Last modification date: 2024-11-06) |
| Primary citation | Nott, T.J.,Kelly, G.,Stach, L.,Li, J.,Westcott, S.,Patel, D.,Hunt, D.M.,Howell, S.,Buxton, R.S.,O'Hare, H.M.,Smerdon, S.J. An intramolecular switch regulates phosphoindependent FHA domain interactions in Mycobacterium tuberculosis. Sci.Signal., 2:ra12-ra12, 2009 Cited by PubMed Abstract: Forkhead-associated (FHA) domains have gained considerable prominence as ubiquitous phosphothreonine-dependent binding modules; however, their precise roles in serine and threonine kinase (STK) pathways and mechanisms of regulation remain unclear. From experiments with Rv1827, an FHA domain-containing protein from Mycobacterium tuberculosis, we derived a complete molecular description of an FHA-mediated STK signaling process. First, binding of the FHA domain to each of three metabolic enzyme complexes regulated their catalytic activities but did not require priming phosphorylation. However, phosphorylation of a threonine residue within a conserved amino-terminal motif of Rv1827 triggered its intramolecular association with the FHA domain of Rv1827, thus blocking its interactions with each of the three enzymes. The solution structure of this inactivated form and further mutagenic studies showed how a previously unidentified intramolecular phosphoswitch blocked the access of the target enzymes to a common FHA interaction surface and how this shared surface accommodated three functionally related, but structurally diverse, binding partners. Thus, our data reveal an unsuspected versatility in the FHA domain that allows for the transformation of multiple kinase inputs into various downstream regulatory signals. PubMed: 19318624DOI: 10.1126/scisignal.2000212 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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