1 * 40800 + 2 * 28700 + 2 * 24500, complete structure of the native enzyme from soybean contains ten molecules of the pentameric enzyme, SDS-PAGE, amino acid analysis
the BnaDGAT1 N-terminal region is required for interactions leading to the dimeric enzyme form, which may allow it to partially mediate positive cooperativity through intermolecular interaction
analysis of self-associating properties of BnDGAT1(1116)His6 in an gel filtration approach, the recombinant N-terminal fragment associates to form tetramers
the full-length polypeptide is predominantly well folded (about 68% alpha-helices/beta-sheets), while the N-terminal domain only has about 29% alpha-helices/beta-sheets
the full-length polypeptide is predominantly well folded (about 68% alpha-helices/beta-sheets), while the N-terminal domain only has about 29% alpha-helices/beta-sheets
the N-terminal region of DGAT1 forms dimers and tetramers based on crosslinking experiments. The N-terminal region plays a role in self-oligomerization. N-terminal structure-function analysis of Brassica napus DGAT1, overview. The remainder of DGAT1 accounting for more than 75% of the enzyme contains the transmembrane dommain (TMD) and the catalytic sites. The TMD is expected to form helical bundles in the membrane, which agrees with the circular dichroism profile of purified BnaDGAT1 indicating the predominance of alpha-helices
the N-terminal region of DGAT1 forms dimers and tetramers based on crosslinking experiments. The N-terminal region plays a role in self-oligomerization. N-terminal structure-function analysis of Brassica napus DGAT1, overview. The remainder of DGAT1 accounting for more than 75% of the enzyme contains the transmembrane dommain (TMD) and the catalytic sites. The TMD is expected to form helical bundles in the membrane, which agrees with the circular dichroism profile of purified BnaDGAT1 indicating the predominance of alpha-helices
the N-terminal region of DGAT1 forms dimers and tetramers based on crosslinking experiments. The N-terminal region plays a role in self-oligomerization. N-terminal structure-function analysis of Brassica napus DGAT1, overview. The remainder of DGAT1 accounting for more than 75% of the enzyme contains the transmembrane dommain (TMD) and the catalytic sites. The TMD is expected to form helical bundles in the membrane, which agrees with the circular dichroism profile of purified BnaDGAT1 indicating the predominance of alpha-helices
isozyme CzDGAT2C contains a short N-terminal hydrophilic tail (3 amino acid), followed by 2 adjacent transmembrane domains (positions 4-23 and 30-52) and a large C-terminal hydrophilic fragment
isozyme CzDGAT2C contains a short N-terminal hydrophilic tail (3 amino acid), followed by 2 adjacent transmembrane domains (positions 4-23 and 30-52) and a large C-terminal hydrophilic fragment
isozyme CzDGAT2C contains a short N-terminal hydrophilic tail (3 amino acid), followed by 2 adjacent transmembrane domains (positions 4-23 and 30-52) and a large C-terminal hydrophilic fragment
the enzyme protein structure is composed of a strongly hydrophilic N-terminal region of about 120 amino acids in MtDGAT1 followed by a long hydrophobic stretch (ca. 400 residues) with a predicted arrangement of 9-10 transmembrane helices that are likely to anchor the protein to the endoplasmic reticulum (ER) membrane
the enzyme protein structure is composed of a strongly hydrophilic N-terminal region of about 120 amino acids in MtDGAT1 followed by a long hydrophobic stretch (ca. 400 residues) with a predicted arrangement of 9-10 transmembrane helices that are likely to anchor the protein to the endoplasmic reticulum (ER) membrane
individual isoform DGAT2 subunits are capable of interacting as part of a multimeric complex. Multiple domains, both in the N and C termini, mediate subunit interaction
individual isoform DGAT2 subunits are capable of interacting as part of a multimeric complex. Multiple domains, both in the N and C termini, mediate subunit interaction
three-dimensional model of the tDGAT protein, structure homology modeling. tDGAT is predicted to have an acyl-CoA-dependent acyltransferase fold, with two domains connected by a helical linker. The core of the predicted N-terminal domain contains a four-stranded mixed sheet (beta2, beta5, beta6 and beta7) surrounded by three alpha-helices (alpha2, alpha4 and alpha5). The core of the predicted C-terminal domain consists of a five-stranded mixed sheet (beta8, beta9, beta10, beta11 and beta12) and five alpha-helices (alpha9, alpha10, alpha11, alpha13 and alpha14) covering the external face of the mixed sheet
three-dimensional model of the tDGAT protein, structure homology modeling. tDGAT is predicted to have an acyl-CoA-dependent acyltransferase fold, with two domains connected by a helical linker. The core of the predicted N-terminal domain contains a four-stranded mixed sheet (beta2, beta5, beta6 and beta7) surrounded by three alpha-helices (alpha2, alpha4 and alpha5). The core of the predicted C-terminal domain consists of a five-stranded mixed sheet (beta8, beta9, beta10, beta11 and beta12) and five alpha-helices (alpha9, alpha10, alpha11, alpha13 and alpha14) covering the external face of the mixed sheet
three-dimensional model of the tDGAT protein, structure homology modeling. tDGAT is predicted to have an acyl-CoA-dependent acyltransferase fold, with two domains connected by a helical linker. The core of the predicted N-terminal domain contains a four-stranded mixed sheet (beta2, beta5, beta6 and beta7) surrounded by three alpha-helices (alpha2, alpha4 and alpha5). The core of the predicted C-terminal domain consists of a five-stranded mixed sheet (beta8, beta9, beta10, beta11 and beta12) and five alpha-helices (alpha9, alpha10, alpha11, alpha13 and alpha14) covering the external face of the mixed sheet