1FQW

CRYSTAL STRUCTURE OF ACTIVATED CHEY

1FQW の概要

• エントリーDOI: 10.2210/pdb1fqw/pdb
• 関連するPDBエントリー: 1C4W 1D5W 1DJM 1QMP
• 分子名称: CHEMOTAXIS CHEY PROTEIN, MANGANESE (II) ION, BERYLLIUM TRIFLUORIDE ION, ... (4 entities in total)
• 機能のキーワード: response regulator, activated chey, chemotaxis, two-component signal transduction, bef3, receiver domain, signaling protein
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 28204.16

構造登録者

Lee, S.Y.,Cho, H.S.,Pelton, J.G.,Yan, D.,Berry, E.A.,Wemmer, D.E. (登録日: 2000-09-07, 公開日: 2001-07-18, 最終更新日: 2024-02-07)

主引用文献

Lee, S.Y.,Cho, H.S.,Pelton, J.G.,Yan, D.,Berry, E.A.,Wemmer, D.E.
Crystal structure of activated CheY. Comparison with other activated receiver domains.
J.Biol.Chem., 276:16425-16431, 2001

PubMed Abstract: 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.

PubMed: 11279165
DOI: 10.1074/jbc.M101002200

実験手法

X-RAY DIFFRACTION (2.37 Å)