2PZZ

2.2 A resolution crystal structure of UPF0201 protein from Methanococcus jannaschii

2PZZ の概要

• エントリーDOI: 10.2210/pdb2pzz/pdb
• 関連するPDBエントリー: 2NRQ 2NWU 2OGK
• 分子名称: UPF0201 protein MJ1564 (2 entities in total)
• 機能のキーワード: upf0201, mj1564, 10077a3, methanococcus jannaschii, psi2, nysgxrc, structural genomics, protein structure initiative, new york sgx research center for structural genomics, unknown function
• 由来する生物種: Methanocaldococcus jannaschii DSM 2661
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 67584.09

構造登録者

Rao, K.N.,Burley, S.K.,Swaminathan, S.,New York SGX Research Center for Structural Genomics (NYSGXRC) (登録日: 2007-05-18, 公開日: 2007-05-29, 最終更新日: 2024-10-16)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.2 Å)