1zu4 | pdb_00001zu4

Crystal structure of FtsY from Mycoplasma mycoides- space group P21212

spinqualitylabelsall models 1zu4, resolution 1.95Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1zu4 is a 1 chain structure with sequence from "asterococcus_mycoides"_borrel_et_al._1910 "asterococcus mycoides" borrel et al. 1910. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: SO4 Related: 1zu5 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Signal recognition particle receptor

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