3sl2

ATP Forms a Stable Complex with the Essential Histidine Kinase WalK (YycG) Domain

spinqualitylabelsall models 3sl2, resolution 1.61Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3sl2 is a 1 chain structure with sequence from "vibrio_subtilis"_ehrenberg_1835 "vibrio subtilis" ehrenberg 1835. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ATP, MG Gene: yycG, BSU40400 ("Vibrio subtilis" Ehrenberg 1835) Activity: Histidine kinase, with EC number 2.7.13.3 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [YYCG_BACSU] Member of the two-component regulatory system YycG/YycF involved in the regulation of the ftsAZ operon, the yocH and ykvT, cwlO, lytE, ydjM, yjeA, yoeB genes and the tagAB and tagDEF operons. Probably phosphorylates YycF. Publication Abstract from PubMed In Bacillus subtilis, the WalRK (YycFG) two-component system coordinates murein synthesis with cell division. It regulates the expression of autolysins that function in cell-wall remodeling and of proteins that modulate autolysin activity. The transcription factor WalR is activated upon phosphorylation by the histidine kinase WalK, a multi-domain homodimer. It autophosphorylates one of its histidine residues by transferring the gamma-phosphate from ATP bound to its ATP-binding domain. Here, the high-resolution crystal structure of the ATP-binding domain of WalK in complex with ATP is presented at 1.61 A resolution. The bound ATP remains intact in the crystal lattice. It appears that the strong binding interactions and the nature of the binding pocket contribute to its stability. The triphosphate moiety of ATP wraps around an Mg(2+) ion, providing three O atoms for coordination in a near-ideal octahedral geometry. The ATP molecule also makes strong interactions with the protein. In addition, there is a short contact between the exocyclic O3' of the sugar ring and O2B of the beta-phosphate, implying an internal hydrogen bond. The stability of the WalK-ATP complex in the crystal lattice suggests that such a complex may exist in vivo poised for initiation of signal transmission. This feature may therefore be part of the sensing mechanism by which the WalRK two-component system is so rapidly activated when cells encounter conditions conducive for growth. ATP forms a stable complex with the essential histidine kinase WalK (YycG) domain.,Celikel R, Veldore VH, Mathews I, Devine KM, Varughese KI Acta Crystallogr D Biol Crystallogr. 2012 Jul;68(Pt 7):839-45. doi:, 10.1107/S090744491201373X. Epub 2012 Jun 15. PMID:22751669 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA