2Q9C

Structure of FTSY:GMPPNP with MGCL Complex

Summary for 2Q9C

• Entry DOI: 10.2210/pdb2q9c/pdb
• Related: 2Q9A 2Q9B
• Descriptor: Cell division protein ftsY, SULFATE ION, PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER, ... (4 entities in total)
• Functional Keywords: inner membrane, ribonucleoprotein, nucleotide-binding, signal recognition particle, srp, gdp, ffh, ftsy, gtpase, rna-binding, gtp-binding, cell division, membrane, cell cycle, signaling protein
• Biological source: Thermus aquaticus
• Cellular location: Cell inner membrane; Peripheral membrane protein (By similarity): P83749
• Total number of polymer chains: 2
• Total formula weight: 67497.55

Authors

Reyes, C.L.,Stroud, R.M. (deposition date: 2007-06-12, release date: 2007-07-03, Last modification date: 2024-02-21)

Primary citation

Reyes, C.L.,Rutenber, E.,Walter, P.,Stroud, R.M.
X-ray Structures of the Signal Recognition Particle Receptor Reveal Targeting Cycle Intermediates.
Plos One, 2:e607-e607, 2007

PubMed Abstract: The signal recognition particle (SRP) and its conjugate receptor (SR) mediate cotranslational targeting of a subclass of proteins destined for secretion to the endoplasmic reticulum membrane in eukaryotes or to the plasma membrane in prokaryotes. Conserved active site residues in the GTPase domains of both SRP and SR mediate discrete conformational changes during formation and dissociation of the SRP.SR complex. Here, we describe structures of the prokaryotic SR, FtsY, as an apo protein and in two different complexes with a non-hydrolysable GTP analog (GMPPNP). These structures reveal intermediate conformations of FtsY containing GMPPNP and explain how the conserved active site residues position the nucleotide into a non-catalytic conformation. The basis for the lower specificity of binding of nucleotide in FtsY prior to heterodimerization with the SRP conjugate Ffh is also shown. We propose that these structural changes represent discrete conformational states assumed by FtsY during targeting complex formation and dissociation.

PubMed: 17622352
DOI: 10.1371/journal.pone.0000607

Experimental method

X-RAY DIFFRACTION (2.2 Å)