2FV2

Crystal Structure Analysis of human Rcd-1 conserved region

Summary for 2FV2

• Entry DOI: 10.2210/pdb2fv2/pdb
• Descriptor: RCD1 required for cell differentiation1 homolog, MANGANESE (II) ION (3 entities in total)
• Functional Keywords: armadillo-repeat, transcription
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 4
• Total formula weight: 122140.94

Authors

Garces, R.G.,Gillon, W.,Pai, E.F. (deposition date: 2006-01-28, release date: 2007-01-09, Last modification date: 2024-02-14)

Primary citation

Garces, R.G.,Gillon, W.,Pai, E.F.
Atomic model of human Rcd-1 reveals an armadillo-like-repeat protein with in vitro nucleic acid binding properties.
Protein Sci., 16:176-188, 2007

PubMed Abstract: Rcd-1, a protein highly conserved across eukaryotes, was initially identified as a factor essential for nitrogen starvation-invoked differentiation in fission yeast, and its Saccharomyces cerevisiae homolog, CAF40, has been identified as part of the CCR4-NOT transcription complex, where it interacts with the NOT1 protein. Mammalian homologs are involved in various cellular differentiation processes including retinoic acid-induced differentiation and hematopoetic cell development. Here, we present the 2.2 A X-ray structure of the highly conserved region of human Rcd-1 and investigate possible functional abilities of this and the full-length protein. The monomer is made up of six armadillo repeats forming a solvent-accessible, positively-charged cleft 21-22 A wide that, in contrast to other armadillo proteins, stays fully exposed in the dimer. Prompted by this finding, we established that Rcd-1 can bind to single- and double-stranded oligonucleotides in vitro with the affinity of G/C/T >> A. Mutation of an arginine residue within the cleft strongly reduced or abolished oligonucleotide binding. Rcd-1's ability to bind to nucleic acids, in addition to the previously reported protein-protein interaction with NOT1, suggests a new feature in Rcd-1's role in regulation of overall cellular differentiation processes.

PubMed: 17189474
DOI: 10.1110/ps.062600507

Experimental method

X-RAY DIFFRACTION (2.2 Å)