ArticleThe EMBO journal2003
Transcarboxylase 12S crystal structure: hexamer assembly and substrate binding to a multienzyme core.
Article in The EMBO journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
12 citing papers in PubMed, 46 citations in OpenAlex.
- Propionic acidemia as a cause of adult-onset dilated cardiomyopathy.European journal of human genetics : EJHG · 2017Article
- Structure and function of biotin-dependent carboxylases.Cellular and molecular life sciences : CMLS · 2013Review
- The enzymes of biotin dependent CO₂ metabolism: what structures reveal about their reaction mechanisms.Protein science : a publication of the Protein Society · 2012Review
- Mechanism of the intramolecular Claisen condensation reaction catalyzed by MenB, a crotonase superfamily member.Biochemistry · 2011Article
- Fatty acid biosynthesis in actinomycetes.FEMS microbiology reviews · 2011Review
- Crystal structure of the alpha(6)beta(6) holoenzyme of propionyl-coenzyme A carboxylase.Nature · 2010Article
- An asymmetric model for Na+-translocating glutaconyl-CoA decarboxylases.The Journal of biological chemistry · 2009Article
- Structural and biophysical characterization of BoxC from Burkholderia xenovorans LB400: a novel ring-cleaving enzyme in the crotonase superfamily.The Journal of biological chemistry · 2009Article
- Crystallization and preliminary crystallographic analysis of DtsR1, a carboxyltransferase subunit of acetyl-CoA carboxylase from Corynebacterium glutamicum.Acta crystallographica. Section F, Structural biology and crystallization communications · 2007Article
- Structure-based inhibitor design of AccD5, an essential acyl-CoA carboxylase carboxyltransferase domain of Mycobacterium tuberculosis.Proceedings of the National Academy of Sciences of the United States of America · 2006Article
- Transcarboxylase 5S structures: assembly and catalytic mechanism of a multienzyme complex subunit.The EMBO journal · 2004Article
- Proteins can convert to beta-sheet in single crystals.Protein science : a publication of the Protein Society · 2004Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
Transcarboxylase from Propionibacterium shermanii is a 1.2 MDa multienzyme complex that couples two carboxylation reactions, transferring CO(2)(-) from methylmalonyl-CoA to pyruvate, yielding propionyl-CoA and oxaloacetate. The 1.9 A resolution crystal structure of the central 12S hexameric core, which catalyzes the first carboxylation reaction, has been solved bound to its substrate methylmalonyl-CoA. Overall, the structure reveals two stacked trimers related by 2-fold symmetry, and a domain duplication in the monomer. In the active site, the labile carboxylate group of methylmalonyl-CoA is stabilized by interaction with the N-termini of two alpha-helices. The 12S domains are structurally similar to the crotonase/isomerase superfamily, although only domain 1 of each 12S monomer binds ligand. The 12S reaction is similar to that of human propionyl-CoA carboxylase, whose beta-subunit has 50% sequence identity with 12S. A homology model of the propionyl-CoA carboxylase beta-subunit, based on this 12S crystal structure, provides new insight into the propionyl-CoA carboxylase mechanism, its oligomeric structure and the molecular basis of mutations responsible for enzyme deficiency in propionic acidemia.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.