Member database | CATH-Gene3D |
CATH-Gene3D type | homologous superfamily |
Description Imported from IPR046363
Malate synthase (MS) (
2.3.3.9) catalyses the aldol condensation of glyoxylate with acetyl-CoA to form malate as part of the second step of the glyoxylate bypass and an alternative to the tricarboxylic acid cycle in bacteria, fungi and plants. There have been identified two isoforms, A and G (MSA and MSG, respectively) that differ in size and is attributed to an inserted α/β domain in MSG that may have regulatory function
[3, 2]. MSA and MSG consist of an N-terminal α-helical clasp domain, a central TIM-barrel domain and a C-terminal helical plug domain. In malate synthases, the TIM β/α-barrel fold and the C-terminal helical domain are well conserved and the cleft between them forms the active site
[3, 2, 1].
This entry covers the N-terminal clasp and the TIM-barrel domains of malate synthases.
References Imported from IPR046363
1.Crystal structure of Escherichia coli malate synthase G complexed with magnesium and glyoxylate at 2.0 A resolution: mechanistic implications. Howard BR, Endrizzi JA, Remington SJ. Biochemistry 39, 3156-68, (2000). View articlePMID: 10715138
2.Structure of the Escherichia coli malate synthase G:pyruvate:acetyl-coenzyme A abortive ternary complex at 1.95 A resolution. Anstrom DM, Kallio K, Remington SJ. Protein Sci. 12, 1822-32, (2003). View articlePMID: 12930982
3.Atomic resolution structures of Escherichia coli and Bacillus anthracis malate synthase A: comparison with isoform G and implications for structure-based drug discovery. Lohman JR, Olson AC, Remington SJ. Protein Sci. 17, 1935-45, (2008). View articlePMID: 18714089
Integrated to
External Links
Representative structure
5oas: Crystal structure of malate synthase G from Pseudomonas aeruginosa in apo form.