2CNW

GDPALF4 complex of the SRP GTPases Ffh and FtsY

Summary for 2CNW

• Entry DOI: 10.2210/pdb2cnw/pdb
• Related: 1FFH 1JPJ 1JPN 1LS1 1NG1 1O87 1OKK 1RJ9 1RY1 2BQS 2BQT 2C03 2C04 2FFH 2J45 2J46 2NG1 3NG1
• Descriptor: SIGNAL RECOGNITION PARTICLE PROTEIN, CELL DIVISION PROTEIN FTSY, GUANOSINE-5'-DIPHOSPHATE, ... (7 entities in total)
• Functional Keywords: inner membrane, membrane targeting, nucleotide-binding, gdp- aluminum fluoride, signal recognition particle, rna-binding, gtp-binding, cell division, signal sequence recognition, srp, ffh, ftsy, gtpase, membrane, cell cycle, cell division-complex, signal recognition
• Biological source: THERMUS AQUATICUS; More
• Cellular location: Cell inner membrane; Peripheral membrane protein (By similarity): P83749
• Total number of polymer chains: 6
• Total formula weight: 193707.42

Authors

Focia, P.J.,Gawronski-Salerno, J.,Coon V, J.S.,Freymann, D.M. (deposition date: 2006-05-24, release date: 2006-10-11, Last modification date: 2023-12-13)

Primary citation

Focia, P.J.,Gawronski-Salerno, J.,Coon V, J.S.,Freymann, D.M.
Structure of a Gdp:Alf(4) Complex of the Srp Gtpases Ffh and Ftsy, and Identification of a Peripheral Nucleotide Interaction Site.
J.Mol.Biol., 360:631-, 2006

PubMed Abstract: The signal recognition particle (SRP) GTPases Ffh and FtsY play a central role in co-translational targeting of proteins, assembling in a GTP-dependent manner to generate the SRP targeting complex at the membrane. A suite of residues in FtsY have been identified that are essential for the hydrolysis of GTP that accompanies disengagement. We have argued previously on structural grounds that this region mediates interactions that serve to activate the complex for disengagement and term it the activation region. We report here the structure of a complex of the SRP GTPases formed in the presence of GDP:AlF4. This complex accommodates the putative transition-state analog without undergoing significant change from the structure of the ground-state complex formed in the presence of the GTP analog GMPPCP. However, small shifts that do occur within the shared catalytic chamber may be functionally important. Remarkably, an external nucleotide interaction site was identified at the activation region, revealed by an unexpected contaminating GMP molecule bound adjacent to the catalytic chamber. This site exhibits conserved sequence and structural features that suggest a direct interaction with RNA plays a role in regulating the activity of the SRP targeting complex.

PubMed: 16780874
DOI: 10.1016/J.JMB.2006.05.031

Experimental method

X-RAY DIFFRACTION (2.39 Å)