5CB0

Crystal structure and functional implications of the tandem-type universal stress protein UspE from Escherichia coli

Summary for 5CB0

• Entry DOI: 10.2210/pdb5cb0/pdb
• Descriptor: Universal stress protein E, 3-oxotetradecanoic acid (2 entities in total)
• Functional Keywords: uspe, uspa superfamily, enterohemorrhagic escherichia coli, unknown function
• Biological source: Escherichia coli
• Cellular location: Cytoplasm : P0AAC0
• Total number of polymer chains: 2
• Total formula weight: 71980.22

Authors

Xu, Y.,Quan, C.S.,Jin, X.,Jin, L.,Kim, J.S.,Guo, J.,Fan, S.,Ha, N.C. (deposition date: 2015-06-30, release date: 2016-02-10, Last modification date: 2023-11-08)

Primary citation

Xu, Y.,Guo, J.,Jin, X.,Kim, J.S.,Ji, Y.,Fan, S.,Ha, N.C.,Quan, C.S.
Crystal structure and functional implications of the tandem-type universal stress protein UspE from Escherichia coli.
Bmc Struct.Biol., 16:3-3, 2016

PubMed Abstract: The universal stress proteins (USP) family member UspE is a tandem-type USP that consists of two Usp domains. The UspE expression levels of the Escherichia coli (E. coli) become elevated in response to oxidative stress and DNA damaging agents, including exposure to mitomycin C, cadmium, and hydrogen peroxide. It has been shown that UspA family members are survival factors during cellular growth arrest. The structures and functions of the UspA family members control the growth of E. coli in animal hosts. While several UspA family members have known structures, the structure of E. coli UspE remains to be elucidated.

PubMed: 26865045
DOI: 10.1186/s12900-016-0053-9

Experimental method

X-RAY DIFFRACTION (3.207 Å)