[NMR paper] Solution NMR studies of sterol carrier protein 2 like 2 (SCP2L2) reveal the insecticide specific structural characteristics of SCP2 proteins in Aedes Aegypti mosquitoes.
Solution NMR studies of sterol carrier protein 2 like 2 (SCP2L2) reveal the insecticide specific structural characteristics of SCP2 proteins in Aedes Aegypti mosquitoes.
Related ArticlesSolution NMR studies of sterol carrier protein 2 like 2 (SCP2L2) reveal the insecticide specific structural characteristics of SCP2 proteins in Aedes Aegypti mosquitoes.
Biochemistry. 2016 Aug 10;
Authors: Singarapu KK, Ahuja A, Potula PR, Ummanni R
Abstract
Sterol carrier protein 2 like 2 from Aedes aegypri (AeSCP2L2) plays an important role in the lipid transport in mosquitoes for its routine metabolic processes. Repeated unsuccessful attempts to crystallize the ligand free SCP2L2 prompted us to undertake NMR spectroscopy to determine its three dimensional structure. We report here the three dimensional structures and dynamics of apo- AeSCP2L2 and its complex with palmitate. 15NHSQC spectrum of apo- AeSCP2L2 displayed multiple peaks for some of the amide resonances inferring the presence of multiple conformations in solution, which are transformed to a single conformation upon complex formation with plamitate. The 3D structures of apo- and palmitated AeSCP2L2 reveal ?/? mixed fold, with five ?-strands and four ?-helices, very similar to the other SCP2 protein structures. Unlike palmitated AeSCP2L2 crystal structure, both the solution structures are monomeric. It is further confirmed by the rotational correlation times determined by NMR relaxation times (T1 and T2) of the amide protons. In addition, the palmitated AeSCP2L2 structure contains two palmitate ligands, bound in the binding pocket, unlike three palmitates bound in dimeric form of AeSCP2L2 in the crystals. The relaxation experiments revealed that the complex formation significantly reduces the dynamics of the protein in solution.
PMID: 27508310 [PubMed - as supplied by publisher]
[NMR paper] NMR structure and function of Helicoverpa armigera sterol carrier protein-2, an important insecticidal target from the cotton bollworm.
NMR structure and function of Helicoverpa armigera sterol carrier protein-2, an important insecticidal target from the cotton bollworm.
NMR structure and function of Helicoverpa armigera sterol carrier protein-2, an important insecticidal target from the cotton bollworm.
Sci Rep. 2015;5:18186
Authors: Ma H, Ma Y, Liu X, Dyer DH, Xu P, Liu K, Lan Q, Hong H, Peng J, Peng R
Abstract
The cotton bollworm, Helicoverpa armigera, has developed strong resistance to many insecticides. Sterol Carrier Protein-2 (SCP-2) is an important...
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[NMR paper] NMR structural studies reveal a novel protein fold for MerB, the organomercurial lyas
NMR structural studies reveal a novel protein fold for MerB, the organomercurial lyase involved in the bacterial mercury resistance system.
Related Articles NMR structural studies reveal a novel protein fold for MerB, the organomercurial lyase involved in the bacterial mercury resistance system.
Biochemistry. 2004 Jul 6;43(26):8322-32
Authors: Di Lello P, Benison GC, Valafar H, Pitts KE, Summers AO, Legault P, Omichinski JG
Mercury resistant bacteria have developed a system of two enzymes (MerA and MerB), which allows them to efficiently...
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[NMR paper] NMR structure of the sterol carrier protein-2: implications for the biological role.
NMR structure of the sterol carrier protein-2: implications for the biological role.
Related Articles NMR structure of the sterol carrier protein-2: implications for the biological role.
J Mol Biol. 2000 Jan 21;295(3):595-603
Authors: García FL, Szyperski T, Dyer JH, Choinowski T, Seedorf U, Hauser H, Wüthrich K
The determination of the NMR structure of the sterol carrier protein-2 (SCP2), analysis of backbone (15)N spin relaxation parameters and NMR studies of nitroxide spin-labeled substrate binding are presented as a new basis for...
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11-18-2010 09:15 PM
[NMR paper] Holo-sterol carrier protein-2. (13)C NMR investigation of cholesterol and fatty acid
Holo-sterol carrier protein-2. (13)C NMR investigation of cholesterol and fatty acid binding sites.
Related Articles Holo-sterol carrier protein-2. (13)C NMR investigation of cholesterol and fatty acid binding sites.
J Biol Chem. 1999 Dec 10;274(50):35425-33
Authors: Stolowich N, Frolov A, Petrescu AD, Scott AI, Billheimer JT, Schroeder F
Although sterol carrier protein-2 (SCP-2) stimulates sterol transfer in vitro, almost nothing is known regarding the identity of the putative cholesterol binding site. Furthermore, the interrelationship(s)...
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NMR and X-ray structures of the putative sterol carrier protein 2 from Thermus thermo
NMR and X-ray structures of the putative sterol carrier protein 2 from Thermus thermophilus HB8 show conformational changes.
Related Articles NMR and X-ray structures of the putative sterol carrier protein 2 from Thermus thermophilus HB8 show conformational changes.
J Struct Funct Genomics. 2010 Oct 5;
Authors: Goroncy AK, Murayama K, Shirouzu M, Kuramitsu S, Kigawa T, Yokoyama S
Sterol carrier protein 2 (SCP-2), also known as nonspecific lipid transfer protein, is a ubiquitous intracellular ~13*kDa protein found in mammals, insects, plants,...
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[NMR paper] The sterol carrier protein-2 fatty acid binding site: an NMR, circular dichroic, and
The sterol carrier protein-2 fatty acid binding site: an NMR, circular dichroic, and fluorescence spectroscopic determination.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles The sterol carrier protein-2 fatty acid binding site: an NMR, circular dichroic, and fluorescence spectroscopic determination.
Biochemistry. 1997 Feb 18;36(7):1719-29
Authors: Stolowich NJ, Frolov A, Atshaves B, Murphy EJ, Jolly CA, Billheimer JT, Scott AI, Schroeder F
The interaction and orientation of fatty acids...
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[NMR paper] The sterol carrier protein-2 fatty acid binding site: an NMR, circular dichroic, and
The sterol carrier protein-2 fatty acid binding site: an NMR, circular dichroic, and fluorescence spectroscopic determination.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles The sterol carrier protein-2 fatty acid binding site: an NMR, circular dichroic, and fluorescence spectroscopic determination.
Biochemistry. 1997 Feb 18;36(7):1719-29
Authors: Stolowich NJ, Frolov A, Atshaves B, Murphy EJ, Jolly CA, Billheimer JT, Scott AI, Schroeder F
The interaction and orientation of fatty acids...
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08-22-2010 03:03 PM
[NMR paper] Solution structural characteristics of cyanometmyoglobin: resonance assignment of hem
Solution structural characteristics of cyanometmyoglobin: resonance assignment of heme cavity residues by two-dimensional NMR.
Related Articles Solution structural characteristics of cyanometmyoglobin: resonance assignment of heme cavity residues by two-dimensional NMR.
Biochemistry. 1990 Feb 13;29(6):1545-56
Authors: Emerson SD, La Mar G
Steady-state nuclear Overhauser effects (NOE), two-dimensional (2D) nuclear Overhauser effect spectroscopy (NOESY), and 2D spin correlation spectroscopy (COSY) have been applied to the fully paramagnetic...