1JPJ

GMPPNP Complex of SRP GTPase NG Domain

Summary for 1JPJ

• Entry DOI: 10.2210/pdb1jpj/pdb
• Related: 1JPN
• Descriptor: SIGNAL RECOGNITION PARTICLE PROTEIN, PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER (3 entities in total)
• Functional Keywords: ffh, srp, gmppnp, signal recognition particle, srp54, ng domain, signaling protein
• Biological source: Thermus aquaticus
• Total number of polymer chains: 1
• Total formula weight: 32994.70

Authors

Padmanabhan, S.,Freymann, D.M. (deposition date: 2001-08-02, release date: 2002-02-02, Last modification date: 2023-08-16)

Primary citation

Padmanabhan, S.,Freymann, D.M.
The conformation of bound GMPPNP suggests a mechanism for gating the active site of the SRP GTPase.
Structure, 9:859-867, 2001

PubMed Abstract: The signal recognition particle (SRP) is a phylogenetically conserved ribonucleoprotein that mediates cotranslational targeting of secreted and membrane proteins to the membrane. Targeting is regulated by GTP binding and hydrolysis events that require direct interaction between structurally homologous "NG" GTPase domains of the SRP signal recognition subunit and its membrane-associated receptor, SR alpha. Structures of both the apo and GDP bound NG domains of the prokaryotic SRP54 homolog, Ffh, and the prokaryotic receptor homolog, FtsY, have been determined. The structural basis for the GTP-dependent interaction between the two proteins, however, remains unknown.

PubMed: 11566135
DOI: 10.1016/S0969-2126(01)00641-4

Experimental method

X-RAY DIFFRACTION (2.3 Å)