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Crystallization and preliminary X‐ray crystallographic analysis of the complex between the N‐D1 domain of VCP from Homo sapiens and the N domain of OTU1 from Saccharomyces cerevisiae
Author(s) -
Kim Su Jin,
Kim Eunice EunKyeong
Publication year - 2014
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x14013351
Subject(s) - homo sapiens , domain (mathematical analysis) , crystallization , saccharomyces cerevisiae , crystallography , computational biology , materials science , biology , chemistry , genetics , gene , mathematics , anthropology , mathematical analysis , organic chemistry , sociology
VCP (valosin‐containing protein; also known as p97) plays important roles in many biological processes including the ERAD (endoplasmic reticulum‐associated degradation) pathway and its function is governed by binding partners. OTU1 (ovarian tumour domain‐containing protein 1) is a recently discovered deubiquitinating enzyme that interacts directly with VCP in the ERAD pathway. In order to understand the interactions between the two proteins, the N‐D1 domain of VCP and the UBXL domain of OTU1 were cloned, overexpressed, purified and crystallized. The crystals of the complex diffracted to 3.25 Å resolution and belonged to space group P 2 1 , with unit‐cell parameters a = 165.45, b = 176.73, c = 165.59 Å, β = 120.095°. There are two molecules of the complex in the asymmetric unit with a Matthews coefficient of 2.62 Å 3 Da −1 and a solvent content of 53%.