5ZXD

Crystal structure of ATP-bound human ABCF1

Summary for 5ZXD

• Entry DOI: 10.2210/pdb5zxd/pdb
• Descriptor: ATP-binding cassette sub-family F member 1, ADENOSINE-5'-TRIPHOSPHATE (3 entities in total)
• Functional Keywords: regulator, translation
• Biological source: Homo sapiens (Human)
• Total number of polymer chains: 2
• Total formula weight: 127168.45

Authors

Qu, L.,Jiang, Y.,Liu, Z.J. (deposition date: 2018-05-18, release date: 2018-07-25, Last modification date: 2024-11-13)

Primary citation

Qu, L.,Jiang, Y.,Cheng, C.,Wu, D.,Meng, B.,Chen, Z.,Zhu, Y.,Shaw, N.,Ouyang, S.,Liu, Z.J.
Crystal Structure of ATP-Bound Human ABCF1 Demonstrates a Unique Conformation of ABC Proteins
Structure, 26:1259-1265.e3, 2018

PubMed Abstract: Gene translation requires the correct selection of start codon AUG in mRNA. ATP-binding cassette subfamily F member 1 (ABCF1) plays a key role in the accuracy of start codon selection. However, the function of human ABCF1 is not clearly understood. Here, we solve the crystal structure of an ATP-bound wild-type human ABCF1 at 2.3-Å resolution. The comparative studies indicate that the structure is in a pre-activation intermediate conformation. This conformation is stabilized by the interaction between ATP and protein. Thus, we propose that this conformation is an important step in the activation of ABCF1. This study extends our understanding of ABC (ATP-binding cassette) protein activation at the molecular level.

PubMed: 30017566
DOI: 10.1016/j.str.2018.05.019

Experimental method

X-RAY DIFFRACTION (2.288 Å)