2OOC

Crystal structure of Histidine Phosphotransferase ShpA (NP_419930.1) from Caulobacter crescentus at 1.52 A resolution

2OOC の概要

• エントリーDOI: 10.2210/pdb2ooc/pdb
• 分子名称: Histidine phosphotransferase, TETRAETHYLENE GLYCOL, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: np_419930.1, hypothetical protein, structural genomics, joint center for structural genomics, jcsg, protein structure initiative, psi-2, transferase
• 由来する生物種: Caulobacter crescentus
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 24925.42

構造登録者

Joint Center for Structural Genomics (JCSG) (登録日: 2007-01-25, 公開日: 2007-02-06, 最終更新日: 2024-10-30)

主引用文献

Xu, Q.,Carlton, D.,Miller, M.D.,Elsliger, M.A.,Krishna, S.S.,Abdubek, P.,Astakhova, T.,Burra, P.,Chiu, H.J.,Clayton, T.,Deller, M.C.,Duan, L.,Elias, Y.,Feuerhelm, J.,Grant, J.C.,Grzechnik, A.,Grzechnik, S.K.,Han, G.W.,Jaroszewski, L.,Jin, K.K.,Klock, H.E.,Knuth, M.W.,Kozbial, P.,Kumar, A.,Marciano, D.,McMullan, D.,Morse, A.T.,Nigoghossian, E.,Okach, L.,Oommachen, S.,Paulsen, J.,Reyes, R.,Rife, C.L.,Sefcovic, N.,Trame, C.,Trout, C.V.,van den Bedem, H.,Weekes, D.,Hodgson, K.O.,Wooley, J.,Deacon, A.M.,Godzik, A.,Lesley, S.A.,Wilson, I.A.
Crystal structure of histidine phosphotransfer protein ShpA, an essential regulator of stalk biogenesis in Caulobacter crescentus.
J.Mol.Biol., 390:686-698, 2009

PubMed Abstract: Cell-cycle-regulated stalk biogenesis in Caulobacter crescentus is controlled by a multistep phosphorelay system consisting of the hybrid histidine kinase ShkA, the histidine phosphotransfer (HPt) protein ShpA, and the response regulator TacA. ShpA shuttles phosphoryl groups between ShkA and TacA. When phosphorylated, TacA triggers a downstream transcription cascade for stalk synthesis in an RpoN-dependent manner. The crystal structure of ShpA was determined to 1.52 A resolution. ShpA belongs to a family of monomeric HPt proteins that feature a highly conserved four-helix bundle. The phosphorylatable histidine His56 is located on the surface of the helix bundle and is fully solvent exposed. One end of the four-helix bundle in ShpA is shorter compared with other characterized HPt proteins, whereas the face that potentially interacts with the response regulators is structurally conserved. Similarities of the interaction surface around the phosphorylation site suggest that ShpA is likely to share a common mechanism for molecular recognition and phosphotransfer with yeast phosphotransfer protein YPD1 despite their low overall sequence similarity.

PubMed: 19450606
DOI: 10.1016/j.jmb.2009.05.023

実験手法

X-RAY DIFFRACTION (1.52 Å)