Aspartate aminotransferase, domain

ALT, alanine aminotransferase ASC, apoptosis-associated speck-like protei containing a CARD AST, aspartate aminotransferase CARD, caspase activation and recruitment domains CD, Crohn s disease COP, CARD-only protein DD, death domain DED, death effector domains DIABLO, direct LAP-binding protein with low pi... 

Arabinose-binding protein domains 1 and 2 Dihydrofolate reductase Adenylate kinase Rhodanese domains 1 and 2 Glutathione reductase domains 1 and 2 Phosphoglycerate mutase Phosphoglycerate kinase domain 2 Pyruvate kinase domain 3 Hexokinase domains 1 and 2 Catalase domain 3 Aspartate aminotransferase... 

Domains 1 and 2 doubly wound parallel fi sheet (Fig. 77) Aspartate aminotransferase (Ford et ah, 1980)... 

Catalytic domain 1 doubly wound parallel fi sheet Catalytic domain 2 classic doubly wound fi sheet (Fig. 76) Aspartate transaminase see Aspartate aminotransferase Aspartate transcarbamylase (Monaco et ah, 1978), see Aspartate carbamoyltransferase... 

Figure 3-23 (A) Stereoscopic a-carbon plot of the cystolic aspartate aminotransferase dimer viewed down its dyad symmetry axis. Bold lines are used for one subunit (subunit 1) and dashed lines for subunit 2. The coenzyme pyridoxal 5 -phosphate (Fig. 3-24) is seen most clearly in subunit 2 (center left). (B) Thirteen sections, spaced 0.1 nm apart, of the 2-methylaspartate difference electron density map superimposed on the a-carbon plot shown in (A). The map is contoured in increments of 2a (the zero level omitted), where a = root mean square density of the entire difference map. Positive difference density is shown as solid contours and negative difference density as dashed contours. The alternating series of negative and positive difference density features in the small domain of subunit 1 (lower right) show that the binding of L-2-methylaspartate between the two domains of this subunit induces a right-to-left movement of the small domain. (Continues)...

Aspartate aminotransferase (AAT) is the first PLP-dependent enzyme for which the three-dimensional structure has been determined " " and is the prototype of fold-type I PLP-enzymes. Each subunit of the AAT homodimer has a large and a small domain. The coenzyme is bound to the large (N-terminal) domain and located in a pocket at the subunit interface, so that residues from each monomer contribute to the formation of both active sites. The proximal and distal carboxylate group of the dicarboxylic substrates bind to Arg386 and Arg292, respectively, the latter contributed by the opposite subunit. " Early crystallographic strucmres... 

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