1sul | pdb_00001sul

Crystal Structure of the apo-YsxC

spinqualitylabelsall models 1sul, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1sul is a 2 chain structure with sequence from "bacillus_globigii"_migula_1900 "bacillus globigii" migula 1900. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 1svi, 1svw Gene: YsxC, ENGB, BSU28190 ("Bacillus globigii" Migula 1900) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [ENGB_BACSU] Necessary for normal cell division and for the maintenance of normal septation (By similarity).[HAMAP-Rule:MF_00321] Binds GTP and GDP.[HAMAP-Rule:MF_00321] 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 Genetic analysis has suggested that the product of the Bacillus subtilis ysxC gene is essential for survival of the microorganism and hence may represent a target for the development of a novel anti-infective agent. B.subtilis YsxC is a member of the translation factor related class of GTPases and its crystal structure has been determined in an apo form and in complex with GDP and GMPPNP/Mg2+. Analysis of these structures has allowed us to examine the conformational changes that occur during the process of nucleotide binding and GTP hydrolysis. These structural changes particularly affect parts of the switch I and switch II region of YsxC, which become ordered and disordered, respectively in the "closed" or "on" GTP-bound state and disordered and ordered, respectively, in the "open" or "off" GDP-bound conformation. Finally, the binding of the magnesium cation results in subtle shifts of residues in the G3 region, at the start of switch II, which serve to optimize the interaction with a key aspartic acid residue. The structural flexibility observed in YsxC is likely to contribute to the role of the protein, possibly allowing transduction of an essential intracellular signal, which may be mediated via interactions with a conserved patch of surface-exposed, basic residues that lies adjacent to the GTP-binding site. Analysis of the open and closed conformations of the GTP-binding protein YsxC from Bacillus subtilis.,Ruzheinikov SN, Das SK, Sedelnikova SE, Baker PJ, Artymiuk PJ, Garcia-Lara J, Foster SJ, Rice DW J Mol Biol. 2004 May 28;339(2):265-78. PMID:15136032 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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