EC Number   |
Subunits |
Reference |
|---|
    3.1.3.15 | ? |
x * 16000-18000, SDS-PAGE |
-, 170814, 170816 |
| 3.1.3.15 | ? |
x * 60000, SDS-PAGE, recombinant GST-fusion protein |
750664 |
| 3.1.3.15 | dimer |
2 * 19903, in the presence of Mg2+ and histidinol phosphate, ESI mass spectrometry |
680722 |
| 3.1.3.15 | dimer |
2 * 28620, recombinant enzyme, SDS-PAGE |
-, 751106 |
| 3.1.3.15 | dimer |
2 * 30378, recombinant enzyme, mass spectrometry, the monomer is with the N-terminal SNA linker that resides after cleavage with tobacco etch virus protease, plus the difference from the two added methylene groups (24 Da) with SNAMSS adduct (577.6 Da) that most probably is an artifact resulting from the MS experiment |
751088 |
| 3.1.3.15 | homotetramer |
4 * 29500, dynamic light scattering |
-, 678231 |
| 3.1.3.15 | homotetramer |
4 * 29976 |
-, 649241 |
| 3.1.3.15 | homotetramer |
4 * 29976, calculated from sequence of cDNA |
-, 678231 |
| 3.1.3.15 | monomer |
1 * 39000, gel filtration |
680523 |
| 3.1.3.15 | More |
covalent dimerization of MtHPP, a monomer of MtHPP has an alphabetaalphabetaalpha-sandwich-like arrangement. The N-terminal domain, which forms an alpha + beta structure, covers residues from the N-terminus to Glu201. Two long alpha-helices (alpha1 and alpha2) are separated by a mobile loop. The eight-stranded beta-sheet of the N-terminal domain contains a alpha-loop motif (residues 131-149), where the beta1 strand is flanked by strands beta2 and beta3. Moreover, a loop between strands beta3 and beta4 encompasses the helix beta3. Strands beta3-beta8 have antiparallel organization. The linker between the N- and C-terminal domains consists of residues between Val202 and Asp209. An extensive interface between the N- and C-terminal domains results in the rigidity of the entire structure, meaning that there is no hinge between the two domains, and they cannot move independently. The C-terminal domain, residues Leu210-Trp326, constitutes an alpha/beta/alpha fold, in which the mixed parallel/antiparallel beta-sheet is sandwiched between helices alpha6, eta7 (310 helix), and alpha8 from one side (close to the beta-sheet of the N-terminal domain) and eta4, alpha5, and alpha9 from the other. MtHPP dimeric assembly is stabilized by intermolecular Lys-CH2-Cys covalent bonds |
751088 |
