1zu5

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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1zu5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zu5 OCA], [http://www.ebi.ac.uk/pdbsum/1zu5 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1zu5 RCSB]</span>
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Revision as of 22:41, 30 March 2008


PDB ID 1zu5

Drag the structure with the mouse to rotate
, resolution 2.40Å
Related: 1ZU4


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Crystal structure of FtsY from Mycoplasma mycoides- space group H32


Overview

The prokaryotic signal recognition particle Ffh and its receptor FtsY allow targeting of proteins into or across the plasma membrane. The targeting process is GTP dependent and the two proteins constitute a distinct GTPase family. The receptor FtsY is composed of A and NG domains where the NG's GTPase domain plays a critical role in the targeting process. In this study, we describe two X-ray structures determined independently of each other of the NG domain of FtsY from Mycoplasma mycoides (MmFtsY). The two structures are markedly different in three of the nucleotide-binding segments, GI (P-loop), GII, and GIII, making only one of the structures compatible with nucleotide binding. Interestingly, the two distinct conformations of the nucleotide-binding segments of MmFtsY are similar to the apo- and ADP-loaded forms of certain ATPases. The structure of the extended interface between the A and NG domains of MmFtsY provides new insights into the role of the A domain for phospholipid interaction.

About this Structure

1ZU5 is a Single protein structure of sequence from Mycoplasma mycoides. Full crystallographic information is available from OCA.

Reference

Conformational variability of the GTPase domain of the signal recognition particle receptor FtsY., Gariani T, Samuelsson T, Sauer-Eriksson AE, J Struct Biol. 2006 Jan;153(1):85-96. Epub 2005 Nov 30. PMID:16343944

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