6NC4

FtsY-NG high-resolution

Summary for 6NC4

• Entry DOI: 10.2210/pdb6nc4/pdb
• Descriptor: Signal recognition particle receptor FtsY, PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER, ACETATE ION, ... (7 entities in total)
• Functional Keywords: ftsy, srp, signal recognition particle receptor, sr, transport protein
• Biological source: Escherichia coli (strain K12)
• Total number of polymer chains: 2
• Total formula weight: 68092.69

Authors

Ataide, S.F.,Faoro, C. (deposition date: 2018-12-10, release date: 2019-10-23, Last modification date: 2024-03-13)

Primary citation

Faoro, C.,Ataide, S.F.
Structural insights into the G-loop dynamics of E. coli FtsY NG domain.
J.Struct.Biol., 208:107387-107387, 2019

PubMed Abstract: The bacterial signal recognition particle (SRP) receptor, FtsY, participates with the SRP in co-translation targeting of proteins. Multiple crystal structures of the NG domain of E. coli FtsY have been determined at high-resolution (1.22-1.88 Å), in the nucleotide-free (apo) form as well as bound to GDP and non-hydrolysable GTP analogues. The combination of high-resolution and multiple solved structures of FtsY in different states revealed a new sensor-relay system of this unique GTPase receptor. A nucleotide sensing function of the P-loop assists FtsY in nucleotide-binding and contributes to modulate nucleotide binding properties in SRP GTPases. A reorganization of the other G-loops and the insertion binding domain (IBD) is observed only upon transition from a diphosphate to a triphosphate nucleotide. The role of a magnesium ion during the GDP and GTP-bound states has also been observed. The binding of magnesium in the nucleotide site causes the reorientation of the β- and γ- phosphate groups toward the jaws of the P-loop and stabilizes the binding of the nucleotide, creating a network of hydrogen and water-bridge interactions.

PubMed: 31520694
DOI: 10.1016/j.jsb.2019.09.004

Experimental method

X-RAY DIFFRACTION (1.6 Å)