PDBsum entry 4zlc

RNA binding protein

PDB id: 4zlc

Contents

Protein chains

155 a.a.

147 a.a.

Waters ×41

PDB id:

4zlc

Name:

RNA binding protein

Title:

Crystal structure of the roq domain of human roquin-2

Structure:

Roquin-2. Chain: a, b, c, d. Fragment: unp residues 171-325. Synonym: membrane-associated nucleic acid-binding protein,ring finger and ccch-type zinc finger domain-containing protein 2,ring finger protein 164. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: rc3h2, mnab, rnf164. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.70Å R-factor: 0.226 R-free: 0.260

Authors:

S.Sakurai,U.Ohto,T.Shimizu

Key ref:

S.Sakurai et al. (2015). Structure of human Roquin-2 and its complex with constitutive-decay element RNA. Acta Crystallogr F Struct Biol Commun, 71, 1048-1054. PubMed id: 26249698 DOI: 10.1107/S2053230X15011887

Date:

01-May-15 Release date: 19-Aug-15

Protein chains

Q9HBD1  (RC3H2_HUMAN) -  Roquin-2 from Homo sapiens

Seq: 1191 a.a.

Struc: 155 a.a.

Protein chains

Q9HBD1  (RC3H2_HUMAN) -  Roquin-2 from Homo sapiens

Seq: 1191 a.a.

Struc: 147 a.a.

Enzyme reactions

• Enzyme class: Chains A, B, C, D: E.C.2.3.2.27 - RING-type E3 ubiquitin transferase.
• Reaction: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N₆- ubiquitinyl-[acceptor protein]-L-lysine

DOI no: 10.1107/S2053230X15011887

Acta Crystallogr F Struct Biol Commun 71:1048-1054 (2015)

PubMed id: 26249698

Structure of human Roquin-2 and its complex with constitutive-decay element RNA.

S.Sakurai, U.Ohto, T.Shimizu.

ABSTRACT

Roquin mediates mRNA degradation by recognizing the constitutive-decay element (CDE) in the 3' untranslated region of the target gene followed by recruitment of the deadenylation machinery. Deficiency or dysfunction of Roquin has been associated with autoimmunity and inflammation. To establish the structural basis for the recognition of CDE RNA by Roquin, the crystal structure of the ROQ domain of human Roquin-2 was determined in ligand-free and CDE-derived RNA-bound forms. The ROQ domain of Roquin-2 folded into a winged-helix structure in which the wing region showed structural flexibility and acted as a lid for RNA binding. The CDE RNA, forming a stem-loop structure, bound to the positively charged surface of the ROQ domain and was mainly recognized via direct interactions with the phosphate backbone in the 5' half of the stem-loop and its triloop and via indirect water-mediated interactions. Structural comparison with Roquin-1 revealed conserved features of the RNA-binding mode. Therefore, it is suggested that the Roquin proteins function redundantly in mRNA degradation.