Computer graphics representation of the ATP- binding domain (reaction site) of phosphoglycerate kinase,a glycolytic enzyme (catalyst). In glycolysis,glucose is converted to pyruvate with the production of ATP: in other words,a catabolic reaction provides metabolic energy (as ATP) at the expense of the degradation of food molecules (glucose). This crystal structure is of horse phosphoglycerate kinase,a bi-lobed structure composed of two domains (one for each reactant),each composed of a six-stranded beta sheet surrounded by alpha helices (blue ribbons). Here,Van der Waals bonded ATP appears in red. This enzyme catalyses the transfer of a phosphoryl group from 1,3-diphosphoglyerate to ADP to yield ATP & 3- phosphoglycerate. Proposed mechanism involves hinge- bending to unite substrates | |
Licence : | Droits gérés |
Crédit: | Science Photo Library / OXFORD MOLECULAR BIOPHYSICS LABORATORY |
Taille de l’image : | 4172 px × 5305 px |
Model Release : | Non requis |
Property Release : | Non requis |
Restrictions : | - |