ArticleThe EMBO journal2000
X-ray structure of MalY from Escherichia coli: a pyridoxal 5'-phosphate-dependent enzyme acting as a modulator in mal gene expression.
Article in The EMBO journal, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 47 citations in OpenAlex.
- Microbial β C-S Lyases: Enzymes with Multifaceted Roles in Flavor Generation.International journal of molecular sciences · 2024Review
- Structural basis for negative regulation of the Escherichia coli maltose system.Nature communications · 2023Article
- A Novel Bifunctional Amino Acid Racemase With Multiple Substrate Specificity, MalY FromFrontiers in microbiology · 2018Article
- Structural Snapshots of an Engineered Cystathionine-γ-lyase Reveal the Critical Role of Electrostatic Interactions in the Active Site.Biochemistry · 2017Article
- Structure of the cystathionine γ-synthase MetB from Mycobacterium ulcerans.Acta crystallographica. Section F, Structural biology and crystallization communications · 2011Article
- Glucose- and glucokinase-controlled mal gene expression in Escherichia coli.Journal of bacteriology · 2009Article
- Crystal structure of Homo sapiens kynureninase.Biochemistry · 2007Article
- Folding pathway of the pyridoxal 5'-phosphate C-S lyase MalY from Escherichia coli.The Biochemical journal · 2005Article
- Identification and functional analysis of Escherichia coli cysteine desulfhydrases.Applied and environmental microbiology · 2005Article
- Evolutionarily conserved regions and hydrophobic contacts at the superfamily level: The case of the fold-type I, pyridoxal-5'-phosphate-dependent enzymes.Protein science : a publication of the Protein Society · 2004Article
- A genomic overview of pyridoxal-phosphate-dependent enzymes.EMBO reports · 2003Review
- A strategy to retrieve the whole set of protein modules in microbial proteomes.Genome research · 2002Article
- The N terminus of the Escherichia coli transcription activator MalT is the domain of interaction with MalY.Journal of bacteriology · 2002Article
- Crystal structure of cystalysin from Treponema denticola: a pyridoxal 5'-phosphate-dependent protein acting as a haemolytic enzyme.The EMBO journal · 2000Article
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Authors and funding
10 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
MalY represents a bifunctional pyridoxal 5'-phosphate-dependent enzyme acting as a beta-cystathionase and as a repressor of the maltose regulon. Here we present the crystal structures of wild-type and A221V mutant protein. Each subunit of the MalY dimer is composed of a large pyridoxal 5'-phosphate-binding domain and a small domain similar to aminotransferases. The structural alignment with related enzymes identifies residues that are generally responsible for beta-lyase activity and depicts a unique binding mode of the pyridoxal 5'-phosphate correlated with a larger, more flexible substrate-binding pocket. In a screen for MalY mutants with reduced mal repressor properties, mutations occurred in three clusters: I, 83-84; II, 181-189 and III, 215-221, which constitute a clearly distinguished region in the MalY crystal structure far away from the cofactor. The tertiary structure of one of these mutants (A221V) demonstrates that positional rearrangements are indeed restricted to regions I, II and III. Therefore, we propose that a direct protein-protein interaction with MalT, the central transcriptional activator of the maltose system, underlies MalY-dependent repression of the maltose system.
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