Crystal structure of 4-hydroxybutyrate CoA-transferase from Clostridium aminobutyricum
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Sofia Macieira
Abstract
4-Hydroxybutyrate CoA-transferases (4-HB-CoAT) takes part in the fermentation of 4-aminobutyrate to ammonia, acetate, and butyrate in anaerobic bacteria such as Clostridium aminobutyricum and Porphyromonas gingivalis or facultative anaerobic bacteria such as Shewanella oneidensis. Site-directed mutagenesis of the highly active enzyme has identified the catalytic glutamate residue as E238. Crystal structure of this enzyme has been determined at a resolution of 1.85 Å. The 438-amino acid residue polypeptide chain folds into two topologically similar domains with an open α/β-fold, which is also found in other CoAT family I and family II members. The data indicate that the members of CoAT families I and II are closely related; the latter only lacking the catalytic glutamate residue. A putative co-substrate binding site for the 4-HB-CoAT was identified, in which a 4-hydroxybutyrate molecule has been modeled. This site is also responsible for binding the acetyl group of acetyl-CoA or the succinyl group of succinyl-CoA in succinyl-CoA:3-oxoacid CoA-transferase from mammalian mitochondria. Mutations of relevant active site amino acid residues have been produced and their activities tested to corroborate the proposed structural model for substrate binding. 4-HB-CoAT from C. aminobutyricum represents the only functionally characterized 4-HB-CoAT present in the structural database.
©2009 by Walter de Gruyter Berlin New York
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- Acknowledgment
- Acknowledgment
- Contents Volume 390, 2009
- Contents Biological Chemistry, Volume 390, 2009
- Author Index
- Author Index
- Subject Index
- Subject Index
Articles in the same Issue
- Reviews
- Chemokines in tumor-associated angiogenesis
- The mammalian aryl hydrocarbon (Ah) receptor: from mediator of dioxin toxicity toward physiological functions in skin and liver
- The mechanism of ATP-dependent RNA unwinding by DEAD box proteins
- Protein Structure and Function
- Crystal structure of 4-hydroxybutyrate CoA-transferase from Clostridium aminobutyricum
- Factors regulating tachyphylaxis triggered by N-terminal-modified angiotensin II analogs
- Cancer Osaka thyroid (Cot) phosphorylates Polo-like kinase (PLK1) at Ser137 but not at Thr210
- Coagulation factor XIII variants with altered thrombin activation rates
- Cell Biology and Signaling
- Stimulation of fibroblast proliferation by the plant cysteine protease CMS2MS2 is independent of its proteolytic activity and requires ERK activation
- EFEMP1 binds the EGF receptor and activates MAPK and Akt pathways in pancreatic carcinoma cells
- Identification of collagen IV derived danger/alarm signals in insect immunity by nanoLC-FTICR MS
- Proteolysis
- Elafin is specifically inactivated by RgpB from Porphyromonas gingivalis by distinct proteolytic cleavage
- Acknowledgment
- Acknowledgment
- Contents Volume 390, 2009
- Contents Biological Chemistry, Volume 390, 2009
- Author Index
- Author Index
- Subject Index
- Subject Index
