PDBsum entry 5xda

Hydrolase

PDB id: 5xda

Contents

Protein chains

(+ 0 more) 537 a.a.

(+ 0 more) 84 a.a.

Waters ×98

PDB id:

5xda

Name:

Hydrolase

Title:

Structural basis for ufm1 recognition by ufsp

Structure:

Ufm1-specific protease. Chain: a, b, c, d, e, f. Fragment: unp residues 25-589. Synonym: ufsp,odorant response abnormal protein 8. Engineered: yes. Mutation: yes. Ubiquitin-fold modifier 1. Chain: g, h, i, j, k, l. Fragment: unp residues 11-94.

Source:

Caenorhabditis elegans. Organism_taxid: 6239. Gene: odr-8, ufsp-2, f38a5.1. Expressed in: escherichia coli. Expression_system_taxid: 562. Gene: ufm-1, tag-277, zk652.3. Expression_system_taxid: 562

Resolution:

3.29Å R-factor: 0.207 R-free: 0.243

Authors:

K.H.Kim,B.H.Ha,E.E.Kim

Key ref:

K.H.Kim et al. (2018). Structural basis for Ufm1 recognition by UfSP. FEBS Lett, 592, 263-273. PubMed id: 29251776 DOI: 10.1002/1873-3468.12951

Date:

28-Mar-17 Release date: 28-Feb-18

Protein chains

Q94218  (UFSP_CAEEL) -  Ufm1-specific protease from Caenorhabditis elegans

Seq: 589 a.a.

Struc: 537 a.a.*

Protein chains

P34661  (UFM1_CAEEL) -  Ubiquitin-fold modifier 1 from Caenorhabditis elegans

Seq: 94 a.a.

Struc: 84 a.a.*

* PDB and UniProt seqs differ at 2 residue positions (black crosses)

Enzyme reactions

• Enzyme class: Chains A, B, C, D, E, F: E.C.3.4.22.- - ?????

DOI no: 10.1002/1873-3468.12951

FEBS Lett 592:263-273 (2018)

PubMed id: 29251776

Structural basis for Ufm1 recognition by UfSP.

K.H.Kim, B.H.Ha, E.E.Kim.

ABSTRACT

Ubiquitin and ubiquitin-like proteins (Ubls) are involved in a variety of cellular functions, and dysfunction of these proteins often leads to disease, thus requiring the precise molecular recognition of the partner. Here, we report a structural basis for the recognition of Ufm1 by the Ufm1-specific protease (UfSP), both from Caenorhabditis elegans. Ufm1 functions in endoplasmic reticulum homeostasis, cell cycle regulation, and dysfunctions of this protein can result in breast cancer and neurological disorders. The structure reveals that in addition to the extended β-structure at the C-terminus of cUfm1, the interactions made by the completely conserved residues in Ufm1 orthologs, Pro88-Val92, corresponding to P6-P2 positions from the cleavage site, seem to be important for the specific recognition of Ufm1 by cUfSP.