Isochorismate pyruvate lyase: Difference between revisions
No edit summary |
No edit summary |
||
| Line 11: | Line 11: | ||
==Structure== | ==Structure== | ||
This is a 101-residue chain made of three alpha helices. Some of the regions overlap with the regions of RdgC base domain which is a DNA binding recombination association protein.The quaternary structure of PchB was found to be dimeric as it is for EcCM (the homologous Chorismate Mutase), and most catalytic residues in the active site of EcCM are conserved in PchB. Moreover, it was shown that pchB complements the CM deficiency of an ''E. coli'' mutant strain and that PchB has low CM activity ''in vitro''. | [[Image:nativeopen.png|300px|left]][[Image:closed.png|300px|left]][[Image:open.png|300px|left]] | ||
This is a 101-residue chain made of three alpha helices. It is found in the apo form, pyruvate bound open anf pyruvate bound closed forms.Some of the regions overlap with the regions of RdgC base domain which is a DNA binding recombination association protein.The quaternary structure of PchB was found to be dimeric as it is for EcCM (the homologous Chorismate Mutase), and most catalytic residues in the active site of EcCM are conserved in PchB. Moreover, it was shown that pchB complements the CM deficiency of an ''E. coli'' mutant strain and that PchB has low CM activity ''in vitro''. | |||
==Chemistry== | ==Chemistry== | ||