Hinge-bending motion in citrate synthase arising from normal mode calculations.
A normal mode analysis of the closed form of dimeric citrate synthase has been performed. The largest-amplitude collective motion predicted by this method compares well with the crystallographically observed hinge-bending motion. Such a result supports those obtained previously in the case of hinge-bending motions of smaller systems, such as lysozyme or hexokinase. Taken together, all these results suggest that low-frequency normal modes may become useful for determining a first approximation of the conformational path between the closed and open forms of these proteins.
Marques
O
O
C.E.R.F.A.C.S., Toulouse, France.
Sanejouand
Y H
YH
D000818:Animals; D002950:Citrate (si)-Synthase / Q000737:chemistry* / Q000378:metabolism; D006593:Hexokinase / Q000737:chemistry; D046911:Macromolecular Substances; D008433:Mathematics; D008958:Models, Molecular; D008962:Models, Theoretical; D009113:Muramidase / Q000737:chemistry; D009206:Myocardium / Q000201:enzymology; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D013552:Swine
D046911:Macromolecular Substances; D002950:Citrate (si)-Synthase; D006593:Hexokinase; D009113:Muramidase