1fqw
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CRYSTAL STRUCTURE OF ACTIVATED CHEY
OverviewOverview
The crystal structure of BeF(3)(-)-activated CheY, with manganese in the, magnesium binding site, was determined at 2.4-A resolution. BeF(3)(-), bonds to Asp(57), the normal site of phosphorylation, forming a hydrogen, bond and salt bridge with Thr(87) and Lys(109), respectively. The six, coordination sites for manganese are satisfied by a fluorine of BeF(3)(-), the side chain oxygens of Asp(13) and Asp(57), the carbonyl oxygen of, Asn(59), and two water molecules. All of the active site interactions seen, for BeF(3)(-)-CheY are also observed in P-Spo0A(r). Thus, BeF(3)(-), activates CheY as well as other receiver domains by mimicking both the, tetrahedral geometry and electrostatic potential of a phosphoryl group., The aromatic ring of Tyr(106) is found buried within a hydrophobic pocket, formed by beta-strand beta4 and helix H4. The tyrosine side chain is, stabilized in this conformation by a hydrogen bond between the hydroxyl, group and the backbone carbonyl oxygen of Glu(89). This hydrogen bond, appears to stabilize the active conformation of the beta4/H4 loop., Comparison of the backbone coordinates for the active and inactive states, of CheY reveals that only modest changes occur upon activation, except in, the loops, with the largest changes occurring in the beta4/H4 loop. This, region is known to be conformationally flexible in inactive CheY and is, part of the surface used by activated CheY for binding its target, FliM., The pattern of activation-induced backbone coordinate changes is similar, to that seen in FixJ(r). A common feature in the active sites of, BeF(3)(-)-CheY, P-Spo0A(r), P-FixJ(r), and phosphono-CheY is a salt bridge, between Lys(109) Nzeta and the phosphate or its equivalent, beryllofluoride. This suggests that, in addition to the concerted, movements of Thr(87) and Tyr(106) (Thr-Tyr coupling), formation of the, Lys(109)-PO(3)(-) salt bridge is directly involved in the activation of, receiver domains generally.
About this StructureAbout this Structure
1FQW is a Single protein structure of sequence from Escherichia coli with MN and BEF as ligands. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of activated CheY. Comparison with other activated receiver domains., Lee SY, Cho HS, Pelton JG, Yan D, Berry EA, Wemmer DE, J Biol Chem. 2001 May 11;276(19):16425-31. Epub 2001 Feb 13. PMID:11279165
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