1RNF

X-RAY CRYSTAL STRUCTURE OF UNLIGANDED HUMAN RIBONUCLEASE 4

1RNF の概要

• エントリーDOI: 10.2210/pdb1rnf/pdb
• 分子名称: PROTEIN (RIBONUCLEASE 4) (2 entities in total)
• 機能のキーワード: hydrolase, ribonuclease, phosphodiesterase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Secreted: P34096
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 27958.07

構造登録者

Terzyan, S.S.,Peracaula, R.,De Llorens, R.,Tsushima, Y.,Yamada, H.,Seno, M.,Gomis-Rueth, F.X.,Coll, M. (登録日: 1998-10-29, 公開日: 1999-10-29, 最終更新日: 2024-11-06)

主引用文献

Terzyan, S.S.,Peracaula, R.,de Llorens, R.,Tsushima, Y.,Yamada, H.,Seno, M.,Gomis-Ruth, F.X.,Coll, M.
The three-dimensional structure of human RNase 4, unliganded and complexed with d(Up), reveals the basis for its uridine selectivity.
J.Mol.Biol., 285:205-214, 1999

PubMed Abstract: The RNase 4 family is unique among RNase enzymes, displaying the highest level of sequence similarity and encompassing the shortest polypeptide chain. It is the only one showing high specificity. The human representative is an intracellular and plasma enzyme, first isolated from colon adenocarcinoma cell line HT-29. The crystal structures of human recombinant RNase 4, unliganded and in complex with d(Up), have been determined, revealing in the unique active site an explanation for the uridine specificity. Arg101, at a position not involved in catalysis in the other RNase enzymes, penetrates the enzyme moiety shaping the recognition pocket, a flip that is mediated by the interaction with the (shorter chain) C-terminal carboxylate group, providing an anchoring point for the O4 atom of the substrate uridine. The bulky Phe42 side-chain forces Asp80 to be in the chi1=-72.49 degrees rotamer, accepting a hydrogen bond from Thr44, further converting the latter into a hydrogen bond acceptor. This favours an interaction with the -NH-donor group of uridine at position 3 over that with the =N-acceptor of cytidine. The two chemical groups that distinguish uracyl from cytosine are used by the enzyme to discriminate between these two bases.

PubMed: 9878400
DOI: 10.1006/jmbi.1998.2288

実験手法

X-RAY DIFFRACTION (2.1 Å)