High Resolution Solution Structure of the 1.3S Subunit of Transcarboxylase from <i>Propionibacterium shermanii</i><sup>†</sup>

Reddy, D V S; Shenoy, Bhami C.; Carey, Paul R.; Sönnichsen, Frank D.

doi:10.1021/bi9925367

Cited by 52 publications

(40 citation statements)

References 34 publications

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“…In contrast to the three-dimensional structure of the biotinoyl domain of E. coli BCCP, the structures of the biotin containing 1.3S subunit of transcarboxylase 61 and the biotinoyl domain of human acetylCoA carboxylase 62 do not contain the ''thumb-like'' motif. Yet, their overall folds are very similar to that of E. coli BCCP.…”

Section: Structure Of the Biotin Carboxyl Carrier Proteinmentioning

confidence: 86%

The enzymes of biotin dependent CO₂ metabolism: What structures reveal about their reaction mechanisms

2012

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Biotin is the major cofactor involved in carbon dioxide metabolism. Indeed, biotindependent enzymes are ubiquitous in nature and are involved in a myriad of metabolic processes including fatty acid synthesis and gluconeogenesis. The cofactor, itself, is composed of a ureido ring, a tetrahydrothiophene ring, and a valeric acid side chain. It is the ureido ring that functions as the CO 2 carrier. A complete understanding of biotin-dependent enzymes is critically important for translational research in light of the fact that some of these enzymes serve as targets for antiobesity agents, antibiotics, and herbicides. Prior to 1990, however, there was a dearth of information regarding the molecular architectures of biotin-dependent enzymes. In recent years there has been an explosion in the number of three-dimensional structures reported for these proteins. Here we review our current understanding of the structures and functions of biotindependent enzymes. In addition, we provide a critical analysis of what these structures have and have not revealed about biotin-dependent catalysis.

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Section: Structure Of the Biotin Carboxyl Carrier Proteinmentioning

confidence: 86%

The enzymes of biotin dependent CO₂ metabolism: What structures reveal about their reaction mechanisms

2012

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“…The N domain and the linker fragment of E. coli BCCP are indispensable for the assembly and function of the acetyl-CoA carboxylase complex in vivo (10,18). Similarly, an active dehydrogenase can never assemble if it lacks the binding domain and the catalytic domain on the E2 component (19).…”

Section: Discussionmentioning

confidence: 99%

“…The other domains are required for them to be functional (10,(17)(18)(19). Here we report the identification and the structural characterization of a single domain protein (GenBank TM accession number NP_570905) with 73 amino acid residues from Bacillus subtilis strain 168.…”

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confidence: 99%

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Identification and Solution Structures of a Single Domain Biotin/Lipoyl Attachment Protein from Bacillus subtilis

Cui

Nan

et al. 2006

Journal of Biological Chemistry

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Protein biotinylation and lipoylation are post-translational modifications, in which biotin or lipoic acid is covalently attached to specific proteins containing biotin/lipoyl attachment domains. All the currently reported natural proteins containing biotin/lipoyl attachment domains are multidomain proteins and can only be modified by either biotin or lipoic acid in vivo. We have identified a single domain protein with 73 amino acid residues from Bacillus subtilis strain 168, and it can be both biotinylated and lipoylated in Escherichia coli. The protein is therefore named as biotin/lipoyl attachment protein (BLAP). This is the first report that a natural single domain protein exists as both a biotin and lipoic acid receptor. The solution structure of apo-BLAP showed that it adopts a typical fold of biotin/lipoyl attachment domain. The structure of biotinylated BLAP revealed that the biotin moiety is covalently attached to the side chain of Lys 35 , and the bicyclic ring of biotin is folded back and immobilized on the protein surface. The biotin moiety immobilization is mainly due to an interaction between the biotin ureido ring and the indole ring of Trp 12 . NMR study also indicated that the lipoyl group of the lipoylated BLAP is also immobilized on the protein surface in a similar fashion as the biotin moiety in the biotinylated protein.The biotin/lipoyl attachment domain (IPR000089) is a signature structural motif, which has a conserved lysine residue that can bind biotin or lipoic acid. This domain can be found in enzymes that require biotin or lipoic acid as cofactor (1). Biotin plays a catalytic role in carboxyl transfer reactions. It is covalently attached to a lysine residue, via an ⑀-amino group, in enzymes such as pyruvate carboxylase, acetyl-CoA carboxylase, and propionyl-CoA carboxylase, etc. (2). This process, called biotinylation, is catalyzed by biotin-protein ligase (BPL) 2 (1, 3).Lipoic acid can serve as cofactor in a variety of proteins, such as E2 acyltransferases (E2p) in the pyruvate dehydrogenase complex and H-protein of the glycine cleavage system (4, 5). It is also covalently bound via an amide linkage to a lysine group. This process, named lipoylation, is catalyzed by lipoate-protein ligase (LPL) (1, 6). It is known that BPLs have broad substrate ranges. Mammalian biotinyl domain can be biotinylated by bacterial BPL and vice versa. The situation for LPLs is also similar (1).The structures of several biotin/lipoyl attachment domains have been determined. Two of them are biotinyl domains, the C-terminal domain of Escherichia coli biotin carboxyl carrier protein (BCCP) and the biotinyl domain of 1.3 S subunit of transcarboxylase from Propionibacterium shermanii (7-10). Several structures of lipoyl domains have also been reported (11-15). All biotinyl domains and lipoyl domains share a very similar overall fold, which is a flattened ␤-barrel formed by two ␤-sheets. The conserved lysine residue is located at the tip of a tight ␤-turn.Although biotinyl and lipoyl domains are quite similar in ...

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“…A similar molecular adaptor-based method was pioneered in our laboratory whereby the 71 amino acid bio tin acceptor peptide (BAP) from Propionibacterium shermanii [Reddy et al, 2000] was genetically fused to the C-termini of the fiber and protein IX , Parrott et al, 2003 as well as into the HVR5 loop of the hexon . The BAP domain is a substrate for endogenous holocarboxylase synthetase (biotin protein ligase) in mammalian cells [Parrott & Barry, 2000] and the resulting Ad-BAP vectors are metabolically biotinylated during production in 293 cells.…”

Section: Combinatorial Approachesmentioning

confidence: 99%

Current Advances and Future Challenges in Adenoviral Vector Biology and Targeting

Campos¹,

Barry²

2007

CGT

172

122

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Gene delivery vectors based on Adenoviral (Ad) vectors have enormous potential for the treatment of both hereditary and acquired disease. Detailed structural analysis of the Ad virion, combined with functional studies has broadened our knowledge of the structure/function relationships between Ad vectors and host cells/tissues and substantial achievement has been made towards a thorough understanding of the biology of Ad vectors. The widespread use of Ad vectors for clinical gene therapy is compromised by their inherent immunogenicity. The generation of safer and more effective Ad vectors, targeted to the site of disease, has therefore become a great ambition in the field of Ad vector development. This review provides a synopsis of the structure/function relationships between Ad vectors and host systems and summarizes the many innovative approaches towards achieving Ad vector targeting.

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High Resolution Solution Structure of the 1.3S Subunit of Transcarboxylase from Propionibacterium shermanii^†

Cited by 52 publications

References 34 publications

The enzymes of biotin dependent CO₂ metabolism: What structures reveal about their reaction mechanisms

The enzymes of biotin dependent CO₂ metabolism: What structures reveal about their reaction mechanisms

Identification and Solution Structures of a Single Domain Biotin/Lipoyl Attachment Protein from Bacillus subtilis

Current Advances and Future Challenges in Adenoviral Vector Biology and Targeting

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High Resolution Solution Structure of the 1.3S Subunit of Transcarboxylase from Propionibacterium shermanii†

Cited by 52 publications

References 34 publications

The enzymes of biotin dependent CO2 metabolism: What structures reveal about their reaction mechanisms

The enzymes of biotin dependent CO2 metabolism: What structures reveal about their reaction mechanisms

Identification and Solution Structures of a Single Domain Biotin/Lipoyl Attachment Protein from Bacillus subtilis

Current Advances and Future Challenges in Adenoviral Vector Biology and Targeting

Contact Info

Product

Resources

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High Resolution Solution Structure of the 1.3S Subunit of Transcarboxylase from Propionibacterium shermanii^†

The enzymes of biotin dependent CO₂ metabolism: What structures reveal about their reaction mechanisms

The enzymes of biotin dependent CO₂ metabolism: What structures reveal about their reaction mechanisms