1yba
From Proteopedia
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The active form of phosphoglycerate dehydrogenase
Overview
An active conformation of phosphoglycerate dehydrogenase (PGDH) from, Escherichia coli has been obtained using X-ray crystallography. The X-ray, crystal structure is used to examine the potential intermediates for, V(max) regulation, for the redox reaction, and for cooperative effects of, serine binding. The crystal structure at 2.2 A resolution contains bound, NAD(+) cofactor, either sulfate or phosphate anions, and, alpha-ketoglutarate, a nonphysiological substrate. A PGDH subunit is, formed from three distinct domains: regulatory (RBD), substrate (SBD), and, nucleotide binding (NBD). The crystal conformation of the homotetramer, points to the fact that, in the absence of serine, coordinated movement of, the RBD-SBD domains occurs relative to the NBD. The result is a, conformational change involving the steric relationships of both the, domains and the subunits. Within the active site of each subunit is a, bound molecule of alpha-ketoglutarate and the coenzyme, NAD. The catalytic, or active site cleft is changed slightly although it is still solvent, exposed; therefore, the catalytic reaction probably involves additional, conformational changes. By comparing the inhibited with the uninhibited, complex, it is possible to describe changes in conformation that are, involved in the inhibitory signal transduction of serine.
About this Structure
1YBA is a Single protein structure of sequence from Escherichia coli with PO4, AKG, UNK and NAD as ligands. Active as Phosphoglycerate dehydrogenase, with EC number 1.1.1.95 Full crystallographic information is available from OCA.
Reference
Vmax regulation through domain and subunit changes. The active form of phosphoglycerate dehydrogenase., Thompson JR, Bell JK, Bratt J, Grant GA, Banaszak LJ, Biochemistry. 2005 Apr 19;44(15):5763-73. PMID:15823035
Page seeded by OCA on Wed Nov 21 06:39:55 2007
