1yqt
From Proteopedia
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RNase-L Inhibitor
Overview
The ABC ATPase RNase-L inhibitor (RLI) emerges as a key enzyme in ribosome, biogenesis, formation of translation preinitiation complexes, and assembly, of HIV capsids. To help reveal the structural mechanism of RLI, we, determined the Mg2+-ADP bound crystal structure of the twin cassette, ATPase of P. furiosus RLI at 1.9 A resolution and analyzed functional, motifs in yeast in vivo. RLI shows similarities but also differences to, known ABC enzyme structures. Twin nucleotide binding domains (NBD1 and, NBD2) are arranged to form two composite active sites in their interface, cleft, indicating they undergo the ATP-driven clamp-like motion of the, NBDs of ABC transporters. An unusual "hinge" domain along the NBD1:NBD2, interface provides a frame for association and possibly ATP-driven, conformational changes of the NBDs. Our results establish a first, structural basis for ABC domain heterodimers and suggest that RLI may act, as mechanochemical enzyme in ribosome and HIV capsid biogenesis.
About this Structure
1YQT is a Single protein structure of sequence from Pyrococcus furiosus with MG and ADP as ligands. Full crystallographic information is available from OCA.
Reference
X-ray structure of RLI, an essential twin cassette ABC ATPase involved in ribosome biogenesis and HIV capsid assembly., Karcher A, Buttner K, Martens B, Jansen RP, Hopfner KP, Structure. 2005 Apr;13(4):649-59. PMID:15837203
Page seeded by OCA on Thu Nov 8 14:37:04 2007
