1RZ4

Crystal Structure of Human eIF3k

Summary for 1RZ4

• Entry DOI: 10.2210/pdb1rz4/pdb
• Descriptor: Eukaryotic translation initiation factor 3 subunit 11, SULFATE ION (3 entities in total)
• Functional Keywords: heat analogous motif, winged-helix, biosynthetic protein
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus: Q9UBQ5
• Total number of polymer chains: 1
• Total formula weight: 26532.21

Authors

Wei, Z.,Zhang, P.,Zhou, Z.,Gong, W. (deposition date: 2003-12-23, release date: 2004-09-21, Last modification date: 2024-10-30)

Primary citation

Wei, Z.,Zhang, P.,Zhou, Z.,Cheng, Z.,Wan, M.,Gong, W.
Crystal structure of human eIF3k, the first structure of eIF3 subunits
J.Biol.Chem., 279:34983-34990, 2004

PubMed Abstract: eIF3k, the smallest subunit of eukaryotic initiation factor 3 (eIF3), interacts with several other subunits of eIF3 and the 40 S ribosomal subunit. eIF3k is conserved among high eukaryotes, including mammals, insects, and plants, and it is ubiquitously expressed in human tissues. Interestingly, eIF3k does not exist in some species of yeast. Thus, eIF3k may play a unique regulatory role in higher organisms. Here we report the crystal structure of human eIF3k, the first high-resolution structure of an eIF3 component. This novel structure contains two distinct domains, a HEAT (named for Huntington, elongation factor 3, A subunit of protein phosphatase 2A, target of rapamycin) repeat-like HAM (HEAT analogous motif) domain and a winged-helix-like WH domain. Through structural comparison and sequence conservation analysis, we show that eIF3k has three putative protein-binding surfaces and has potential RNA binding activity. The structure provides key information for understanding the structure and function of the eIF3 complex.

PubMed: 15180986
DOI: 10.1074/jbc.M405158200

Experimental method

X-RAY DIFFRACTION (2.1 Å)