The structure of the negative transcriptional regulator NmrA reveals a structural superfamily which includes the short-chain dehydrogenase/reductases.

Journal article

NmrA is a negative transcriptional regulator involved in the post-translational modulation of the GATA-type transcription factor AreA, forming part of a system controlling nitrogen metabolite repression in various fungi. X-ray structures of two NmrA crystal forms, both to 1.8 A resolution, show NmrA consists of two domains, including a Rossmann fold. NmrA shows an unexpected similarity to the short-chain dehydrogenase/reductase (SDR) family, with the closest relationship to UDP-galactose 4-ep...

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Authors: Stammers, D; Ren, J; Leslie, K; Nichols, C; Lamb, H

• Publication status: Published
• Journal: EMBO journal
• Volume: 20
• Issue: 23
• Pages: 6619-6626
• Publication date: 2001-12-01
• DOI: 10.1093/emboj/20.23.6619
• EISSN: 1460-2075
• ISSN: 0261-4189
• Language: English
• Keywords: Models, Molecular; Transcription Factors; Fungal Proteins; Catalytic Domain; Transcription, Genetic; Protein Structure, Secondary; Crystallography, X-Ray; Protein Structure, Tertiary; Binding Sites; NAD; Molecular Sequence Data; Electrons; Neurospora crassa; Protein Binding; Protein Folding; UDPglucose 4-Epimerase; Tyrosine; Sequence Homology, Amino Acid; Amino Acid Sequence; Protein Processing, Post-Translational; Repressor Proteins