2PZZ

2.2 A resolution crystal structure of UPF0201 protein from Methanococcus jannaschii

Summary for 2PZZ

• Entry DOI: 10.2210/pdb2pzz/pdb
• Related: 2NRQ 2NWU 2OGK
• Descriptor: UPF0201 protein MJ1564 (2 entities in total)
• Functional Keywords: upf0201, mj1564, 10077a3, methanococcus jannaschii, psi2, nysgxrc, structural genomics, protein structure initiative, new york sgx research center for structural genomics, unknown function
• Biological source: Methanocaldococcus jannaschii DSM 2661
• Total number of polymer chains: 4
• Total formula weight: 67584.09

Authors

Rao, K.N.,Burley, S.K.,Swaminathan, S.,New York SGX Research Center for Structural Genomics (NYSGXRC) (deposition date: 2007-05-18, release date: 2007-05-29, Last modification date: 2024-10-16)

Primary citation

Rao, K.N.,Burley, S.K.,Swaminathan, S.
UPF201 archaeal specific family members reveal structural similarity to RNA-binding proteins but low likelihood for RNA-binding function.
Plos One, 3:e3903-e3903, 2008

PubMed Abstract: We have determined X-ray crystal structures of four members of an archaeal specific family of proteins of unknown function (UPF0201; Pfam classification: DUF54) to advance our understanding of the genetic repertoire of archaea. Despite low pairwise amino acid sequence identities (10-40%) and the absence of conserved sequence motifs, the three-dimensional structures of these proteins are remarkably similar to one another. Their common polypeptide chain fold, encompassing a five-stranded antiparallel beta-sheet and five alpha-helices, proved to be quite unexpectedly similar to that of the RRM-type RNA-binding domain of the ribosomal L5 protein, which is responsible for binding the 5S- rRNA. Structure-based sequence alignments enabled construction of a phylogenetic tree relating UPF0201 family members to L5 ribosomal proteins and other structurally similar RNA binding proteins, thereby expanding our understanding of the evolutionary purview of the RRM superfamily. Analyses of the surfaces of these newly determined UPF0201 structures suggest that they probably do not function as RNA binding proteins, and that this domain specific family of proteins has acquired a novel function in archaebacteria, which awaits experimental elucidation.

PubMed: 19079550
DOI: 10.1371/journal.pone.0003903

Experimental method

X-RAY DIFFRACTION (2.2 Å)