1K6J

Crystal structure of Nmra, a negative transcriptional regulator (Monoclinic form)

Summary for 1K6J

• Entry DOI: 10.2210/pdb1k6j/pdb
• Related: 1K6I
• Descriptor: NmrA, CHLORIDE ION (3 entities in total)
• Functional Keywords: rossmann fold transcriptional regulation short chain dehydrogenase reductase, transcription
• Biological source: Emericella nidulans
• Total number of polymer chains: 2
• Total formula weight: 77918.65

Authors

Stammers, D.K.,Ren, J.,Leslie, K.,Nichols, C.E.,Lamb, H.K.,Cocklin, S.,Dodds, A.,Hawkins, A.R. (deposition date: 2001-10-16, release date: 2002-02-20, Last modification date: 2023-08-16)

Primary citation

Stammers, D.K.,Ren, J.,Leslie, K.,Nichols, C.E.,Lamb, H.K.,Cocklin, S.,Dodds, A.,Hawkins, A.R.
The structure of the negative transcriptional regulator NmrA reveals a structural superfamily which includes the short-chain dehydrogenase/reductases.
EMBO J., 20:6619-6626, 2001

PubMed Abstract: 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-epimerase. We show that NAD binds to NmrA, a previously unreported nucleotide binding property for this protein. NmrA is unlikely to be an active dehydrogenase, however, as the conserved catalytic tyrosine in SDRs is absent in NmrA, and thus the nucleotide binding to NmrA could have a regulatory function. Our results suggest that other transcription factors possess the SDR fold with functions including RNA binding. The SDR fold appears to have been adapted for other roles including non-enzymatic control functions such as transcriptional regulation and is likely to be more widespread than previously recognized.

PubMed: 11726498
DOI: 10.1093/emboj/20.23.6619

Experimental method

X-RAY DIFFRACTION (1.8 Å)