3LMO

Crystal Structure of specialized acyl carrier protein (RPA2022) from Rhodopseudomonas palustris, Northeast Structural Genomics Consortium Target RpR324

3LMO の概要

• エントリーDOI: 10.2210/pdb3lmo/pdb
• 分子名称: Specialized acyl carrier protein (2 entities in total)
• 機能のキーワード: alpha-beta protein, structural genomics, psi-2, protein structure initiative, northeast structural genomics consortium, nesg, phosphopantetheine, transferase
• 由来する生物種: Rhodopseudomonas palustris
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 11309.72

構造登録者

Forouhar, F.,Rossi, P.,Lew, S.,Seetharaman, J.,Mao, M.,Xiao, R.,Ciccosanti, C.,Wang, H.,Everett, J.K.,Nair, R.,Acton, T.B.,Rost, B.,Montelione, G.T.,Tong, L.,Hunt, J.F.,Northeast Structural Genomics Consortium (NESG) (登録日: 2010-01-31, 公開日: 2010-02-16, 最終更新日: 2024-02-21)

主引用文献

Ramelot, T.A.,Rossi, P.,Forouhar, F.,Lee, H.W.,Yang, Y.,Ni, S.,Unser, S.,Lew, S.,Seetharaman, J.,Xiao, R.,Acton, T.B.,Everett, J.K.,Prestegard, J.H.,Hunt, J.F.,Montelione, G.T.,Kennedy, M.A.
Structure of a specialized acyl carrier protein essential for lipid A biosynthesis with very long-chain fatty acids in open and closed conformations.
Biochemistry, 51:7239-7249, 2012

PubMed Abstract: The solution nuclear magnetic resonance (NMR) structures and backbone (15)N dynamics of the specialized acyl carrier protein (ACP), RpAcpXL, from Rhodopseudomonas palustris, in both the apo form and holo form modified by covalent attachment of 4'-phosphopantetheine at S37, are virtually identical, monomeric, and correspond to the closed conformation. The structures have an extra α-helix compared to the archetypical ACP from Escherichia coli, which has four helices, resulting in a larger opening to the hydrophobic cavity. Chemical shift differences between apo- and holo-RpAcpXL indicated some differences in the hinge region between α2 and α3 and in the hydrophobic cavity environment, but corresponding changes in nuclear Overhauser effect cross-peak patterns were not detected. In contrast to the NMR structures, apo-RpAcpXL was observed in an open conformation in crystals that diffracted to 2.0 Å resolution, which resulted from movement of α3. On the basis of the crystal structure, the predicted biological assembly is a homodimer. Although the possible biological significance of dimerization is unknown, there is potential that the resulting large shared hydrophobic cavity could accommodate the very long-chain fatty acid (28-30 carbons) that this specialized ACP is known to synthesize and transfer to lipid A. These structures are the first representatives of the AcpXL family and the first to indicate that dimerization may be important for the function of these specialized ACPs.

PubMed: 22876860
DOI: 10.1021/bi300546b

実験手法

X-RAY DIFFRACTION (2 Å)