2KW2

Solution NMR of the specialized acyl carrier protein (RPA2022) from Rhodopseudomonas palustris, Northeast Structural Genomics Consortium Target RpR324

Summary for 2KW2

• Entry DOI: 10.2210/pdb2kw2/pdb
• Related: 3lmo
• NMR Information: BMRB: 16805
• Descriptor: Specialized acyl carrier protein (1 entity in total)
• Functional Keywords: structural genomics, northeast structural genomics consortium (nesg), psi-2, protein structure initiative, transferase
• Biological source: Rhodopseudomonas palustris
• Total number of polymer chains: 1
• Total formula weight: 11309.72

Authors

Rossi, P.,Lee, H.,Wohlbold, T.J.,Valafar, H.,Lemak, A.,Ertekin, A.,Forouhar, F.,Ciccosanti, C.,Rost, B.,Acton, T.,Xiao, R.,Everett, J.,Montelione, G.T.,Northeast Structural Genomics Consortium (NESG) (deposition date: 2010-03-30, release date: 2010-04-21, Last modification date: 2024-05-01)

Primary citation

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

Experimental method

SOLUTION NMR