2V3M

Structure of the Gar1 domain of NAf1

Summary for 2V3M

• Entry DOI: 10.2210/pdb2v3m/pdb
• Descriptor: NAF1, SULFATE ION (2 entities in total)
• Functional Keywords: ribosomal protein, naf1, gar1, snornp, phosphorylation, hypothetical protein
• Biological source: SACCHAROMYCES CEREVISIAE (BAKER'S YEAST)
• Cellular location: Nucleus: P53919
• Total number of polymer chains: 6
• Total formula weight: 92077.06

Authors

Leulliot, N.,Godin, K.S.,Hoareau-Aveilla, C.,Quevillon-Cheruel, S.,Varani, G.,Henry, Y.,van Tilbeurgh, H. (deposition date: 2007-06-19, release date: 2007-07-10, Last modification date: 2024-11-06)

Primary citation

Leulliot, N.,Godin, K.S.,Hoareau-Aveilla, C.,Quevillon-Cheruel, S.,Varani, G.,Henry, Y.,Van Tilbeurgh, H.
The Box H/Aca Rnp Assembly Factor Naf1P Contains a Domain Homologous to Gar1P Mediating its Interaction with Cbf5P.
J.Mol.Biol., 371:1338-, 2007

PubMed Abstract: Naf1 is an essential protein involved in the maturation of box H/ACA ribonucleoproteins, a group of particles required for ribosome biogenesis, modification of spliceosomal small nuclear RNAs and telomere synthesis. Naf1 participates in the assembly of the RNP at transcription sites and in the nuclear trafficking of the complex. The crystal structure of a domain of yeast Naf1p, Naf1Delta1p, reveals a striking structural homology with the core domain of archaeal Gar1, an essential protein component of the mature RNP; it suggests that Naf1p and Gar1p have a common binding site on the enzymatic protein component of the particle, Cbf5p. We propose that Naf1p is a competitive binder for Cbf5p, which is replaced by Gar1p during maturation of the H/ACA particle. The exchange of Naf1p by Gar1p might be prompted by external factors that alter the oligomerisation state of Naf1p and Gar1p. The structural homology with Gar1 suggests that the function of Naf1 involves preventing non-cognate RNAs from being loaded during transport of the particle by inducing a non-productive conformation of Cbf5.

PubMed: 17612558
DOI: 10.1016/J.JMB.2007.06.031

Experimental method

X-RAY DIFFRACTION (2.74 Å)