2P81
Engrailed homeodomain helix-turn-helix motif
Summary for 2P81
| Entry DOI | 10.2210/pdb2p81/pdb |
| Related | 1ENH 1ZTR |
| NMR Information | BMRB: 7386 |
| Descriptor | Segmentation polarity homeobox protein engrailed (1 entity in total) |
| Functional Keywords | helix-turn-helix motif, motif, engrailed, homeodomain, dna binding, protein folding, intermediate, native, transcription |
| Biological source | Drosophila melanogaster (fruit fly) |
| Cellular location | Nucleus: P02836 |
| Total number of polymer chains | 1 |
| Total formula weight | 5419.21 |
| Authors | Religa, T.L. (deposition date: 2007-03-21, release date: 2007-06-12, Last modification date: 2024-05-22) |
| Primary citation | Religa, T.L.,Johnson, C.M.,Vu, D.M.,Brewer, S.H.,Dyer, R.B.,Fersht, A.R. The helix-turn-helix motif as an ultrafast independently folding domain: The pathway of folding of Engrailed homeodomain. Proc.Natl.Acad.Sci.Usa, 104:9272-9277, 2007 Cited by PubMed Abstract: Helices 2 and 3 of Engrailed homeodomain (EnHD) form a helix-turn-helix (HTH) motif. This common motif is believed not to fold independently, which is the characteristic feature of a motif rather than a domain. But we found that the EnHD HTH motif is monomeric and folded in solution, having essentially the same structure as in full-length protein. It had a sigmoidal thermal denaturation transition. Both native backbone and local tertiary interactions were formed concurrently at 4 x 10(5) s(-1) at 25 degrees C, monitored by IR and fluorescence T-jump kinetics, respectively, the same rate constant as for the fast phase in the folding of EnHD. The HTH motif, thus, is an ultrafast-folding, natural protein domain. Its independent stability and appropriate folding kinetics account for the stepwise folding of EnHD, satisfy fully the criteria for an on-pathway intermediate, and explain the changes in mechanism of folding across the homeodomain family. Experiments on mutated and engineered fragments of the parent protein with different probes allowed the assignment of the observed kinetic phases to specific events to show that EnHD is not an example of one-state downhill folding. PubMed: 17517666DOI: 10.1073/pnas.0703434104 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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