PDBsum entry 4zg0

Hydrolase

PDB id: 4zg0

Contents

Protein chains

191 a.a.

Waters ×259

PDB id:

4zg0

Name:

Hydrolase

Title:

Crystal structure of mouse syndesmos protein

Structure:

Protein syndesmos. Chain: a, b. Fragment: unp residues 8-204. Synonym: nudt16-like protein 1. Engineered: yes

Source:

Mus musculus. Mouse. Organism_taxid: 10090. Gene: nudt16l1, sdos. Expressed in: escherichia coli bl21. Expression_system_taxid: 511693.

Resolution:

2.01Å R-factor: 0.182 R-free: 0.225

Authors:

I.Lee,H.Kim,J.Yoo,H.Cho,W.Lee

Key ref:

H.Kim et al. (2015). Crystal structure of syndesmos and its interaction with Syndecan-4 proteoglycan. Biochem Biophys Res Commun, 463, 762-767. PubMed id: 26100207 DOI: 10.1016/j.bbrc.2015.06.010

Date:

22-Apr-15 Release date: 20-Apr-16

Protein chains

Q8VHN8  (TIRR_MOUSE) -  Tudor-interacting repair regulator protein from Mus musculus

Seq: 211 a.a.

Struc: 191 a.a.

DOI no: 10.1016/j.bbrc.2015.06.010

Biochem Biophys Res Commun 463:762-767 (2015)

PubMed id: 26100207

Crystal structure of syndesmos and its interaction with Syndecan-4 proteoglycan.

H.Kim, J.Yoo, I.Lee, Y.J.Kang, H.S.Cho, W.Lee.

ABSTRACT

Syndesmos, nucleoside diphosphate linked moiety X (nudix)-type motif 16-like 1 (Nudt16l1), is evolutionarily divergent from the Nudt16 family. Syndesmos, which is co-localized with syndecan-4 cytoplasmic domain (Syn4(cyto)) in focal contacts, interacts with various cell adhesion adaptor proteins to control cell signaling. We determined the X-ray crystal structure of syndesmos; it is composed of seven α-helices and seven β-strands. Although syndesmos has a molecular topology similar to that of nudix hydrolase proteins, the structure of the nudix motif differs from that of X29. The dimeric interface of syndesmos is composed of α-helix 4, 7 and β-strand 2, 7, which primarily form hydrophobic interactions. The binding interaction between syndesmos and syn4(cyto) was characterized as a low-affinity interaction (Kd = 62 μM) by surface plasmon resonance (SPR) and nuclear magnetic resonance (NMR). The NMR resonances of Lys (177, 178, 179), Gly182, and Ser183 in the C1 region and Lys193 and Lys194 in the V region of syndecan-4 are perturbed upon syndesmos binding. Our results provide structural insight into the molecular function of syndesmos in the regulation of cell signaling via binding to syndecan-4.