PDBsum entry 2fv2

Transcription

PDB id: 2fv2

Contents

Protein chains

267 a.a. *

Metals

_MN

Waters ×661

* Residue conservation analysis

PDB id:

2fv2

Name:

Transcription

Title:

Crystal structure analysis of human rcd-1 conserved region

Structure:

Rcd1 required for cell differentiation1 homolog. Chain: a, b, c, d. Fragment: (residues: 18 - 285). Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: rcd1. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.20Å R-factor: 0.217 R-free: 0.279

Authors:

R.G.Garces,W.Gillon,E.F.Pai

Key ref:

R.G.Garces et al. (2007). Atomic model of human Rcd-1 reveals an armadillo-like-repeat protein with in vitro nucleic acid binding properties. Protein Sci, 16, 176-188. PubMed id: 17189474 DOI: 10.1110/ps.062600507

Date:

28-Jan-06 Release date: 09-Jan-07

Protein chains

Q92600  (CNOT9_HUMAN) -  CCR4-NOT transcription complex subunit 9 from Homo sapiens

Seq: 299 a.a.

Struc: 267 a.a.

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1110/ps.062600507

Protein Sci 16:176-188 (2007)

PubMed id: 17189474

Atomic model of human Rcd-1 reveals an armadillo-like-repeat protein with in vitro nucleic acid binding properties.

R.G.Garces, W.Gillon, E.F.Pai.

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.

Selected figure(s)

Figure 2.
Figure 2. Structure of hRcd-1 DNC. (A) Stereo ribbon diagram of the dimer. The twofold axis runs approximately horizontal to the

The above figure is reprinted by permission from the Protein Society: Protein Sci (2007, 16, 176-188) copyright 2007.

Figure was selected by an automated process.