The crystal structure of succinyl-CoA synthetase from Escherichia coli at 2.5-A resolution.

Two crystal structures of N-acetyltransferases reveal a new fold for CoA-dependent enzymes

“…It should be noted, however, that the directionality of the nucleotide is reversed: the relative position of the adenine moiety which is 'above' the sheet in Hat1 is 'below' the sheet in the classical mode of binding. So far, only one CoA-dependent enzyme has been shown to have a CoA-binding domain with a Rossmann fold, namely succinyl-CoA synthetase [10]. The mode of CoA binding of this enzyme is shown in Figure 2c.…”

“…Citrate synthase 2cts [17] Dihydrolipoyl transacetylase 1eab [18] Acyl-CoA dehydrogenase 3mde [19] Succinyl-CoA synthetase 1scu [10] Methymalonyl-CoA mutase 1req [20] Enoyl-CoA hydratase 1dub [21] Acyl-CoA-binding protein 1aca [22] 3-Hydroxyacyl-CoA dehydrogenase - [23] Choramphenicol acetyltransferase 1cla [24] 3-Ketoacyl-CoA thiolase 1afw [13] 3-HMG-CoA dehydrogenase - [25] Malonyl-CoA ACP transacylase 1mla [26] 4-Chlorobenzoyl-CoA dehalogenase 1nzy [27] Isovaleryl-CoA dehydrogenase 1ivh [28] Lipid-transfer protein 1jtb [29] Dienoyl-CoA isomerase 1dci [30] N-myristoyl-CoA transferase 1nmt [5] Xenobiotic acetyltransferase 2xat [31] Aminoglycoside 3-N-acetyltransferase - [8] Histone acetyltransferase Hat1 1bob [6] This table includes structures described in the literature before October 1998. Only one Protein Data Bank (PDB) entry code is given for each enzyme, even when more are available.…”

The structure of glucose-fructose oxidoreductase from Zymomonas mobilis: an osmoprotective periplasmic enzyme containing non-dissociable NADP

“…Using the structure comparison algorithm of Holm and Sander [25], we compared the dinucleotide-binding domain of GFOR with structures deposited in the Protein Data Bank. The greatest degree of overall structural similarity was with the coenzyme A binding domain of succinyl-CoA synthetase [26] (rms difference for 107 equivalent C␣ positions: 2.2 Å), and with the NADP-binding domain of DHPR [21] (rms difference for 111 equivalent C␣ positions: 2.2 Å).…”

The nucleotide specificity of succinyl‐CoA synthetase of Plasmodium falciparum is not determined by charged gatekeeper residues alone

“…After identification of the gatekeeper residues from the MSA, various mutants were designed in an attempt to alter the charge of the gatekeeper residues; details are summarized in Table 2. Structure models were generated for the wild‐type (WT) and various mutant Pf SCSβ subunits by using modeler 9v13 (University of California San Francisco, CA, USA), with the following templates, E. coli SCS [Protein Data Bank (PDB): https://doi.org/10.2210/pdb1CQI/pdb] [12] and pig SCS (PDB: https://doi.org/10.2210/pdb2FP4/pdb) [13]. The models were further analyzed by Ramachandran scatterplots and DOPE scores.…”