Protein is shown in colour according to scheme in Fig. Maps are shown at contour level of 0. Maps coloured according to local resolution, colour scale is provided.
Electron microscopy maps are shown at contour level of 0. Labels indicate local resolution estimates for a box size of 40 pixel around the indicated positions, calculated using localfsc in Chimera using either the unfiltered half-maps directly left value or the unfiltered half-maps after local averaging as input right value. Local resolution differentially improves after local averaging.
Map is shown at contour level of 0. Maps in b and c are shown at contour level of 0. Maps in d and f are shown at contour level of 0. Arrows indicate rarely observed, residual, non-polymerized ACC further analysed in c. ACC-like classes are marked in red. A variety of elongated conformations can be observed. Owing to the tetrameric nature of streptavidin, higher-order complexes are formed, which can also be observed on the gel.
An uncropped image of the gel is shown in Supplementary Fig. Due to limited resolution, the cofactor was not modelled; its orientation is shown schematically. For clarity, parts of BCCP are not shown. The map is shown at contour level of 0. Local two-fold symmetry is indicated, and domains of the lower dimer are labelled. ACC—citrate is shown in colour as cartoon representation. Sc ACC is shown as a cartoon in grey and superimposed for one side of the interface.
For the other side, an additional surface representation is shown for ACC—citrate. Residue numbers according to human ACC are indicated as well as the helices, the loops and the strand labelled in b and c. Darker colour indicates increased conservation. Pairwise identity over all aligned sequences is At molar ratio, ACC—citrate palm filaments are observed.
At molar ratio, filaments dissolve. Bottom left, enlarged negative stain electron micrograph of ACC—citrate filament with surface representation of the model coloured according to domains. Bottom right, electron micrograph of a ACC—citrate palm filament and interpretation by a plausible model derived from ACC—citrate filaments by disrupting the BC domain dimers and flipping out of the BC domain. These domains constitute the connecting arms between adjacent nodes.
Left, view without BRCT domains; the phosphosite loops are labelled. Right, view with dimeric BRCT domains establishing the connections between two dimers. The interaction is governed by binding of the phosphosite loop to the dimeric BRCT.
Colouring as in b. The range of displacements of the ends of the bundle is indicated by arrows. Maps in e and g are shown at contour level of 0. This file contains Supplementary Fig. Uncropped gel directly as obtained by scanning shows sizemarker with molecular masses indicated.
The cropped region is indicated by a black square in dashed lines. The gel contains three molecular mass markers and two sets of the same samples, the right set contains half of the amount of protein of the left set. The contrast was enhanced for the gel shown in Fig. Overview of the ACC—citrate filament as well as zoom-in onto an individual, excised ACC dimer, which is in a closed, catalytically active form.
The protomers in the filament as well as the domains in the dimer are indicated. Colour scheme according to Fig. Reprints and Permissions. Structural basis for regulation of human acetyl-CoA carboxylase. Download citation. Received : 02 July Accepted : 24 April Published : 13 June Issue Date : 21 June Anyone you share the following link with will be able to read this content:. Sorry, a shareable link is not currently available for this article. Provided by the Springer Nature SharedIt content-sharing initiative.
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Elliott, J. Kulpa, W. Lee; Regulation of acetyl-CoA carboxylase. Biochem Soc Trans 1 April ; 34 2 : — Acetyl-CoA carboxylase ACC catalyses the formation of malonyl-CoA, an essential substrate for fatty acid synthesis in lipogenic tissues and a key regulatory molecule in muscle, brain and other tissues. ACC contributes importantly to the overall control of energy metabolism and has provided an important model to explore mechanisms of enzyme control and hormone action.
Mammalian ACCs are multifunctional dimeric proteins — kDa with the potential to further polymerize and engage in multiprotein complexes. The enzymatic properties of ACC are complex, especially considering the two active sites, essential catalytic biotin, the three-substrate reaction and effects of allosteric ligands.
The expression of the two major isoforms and splice variants of mammalian ACC is tissue-specific and responsive to hormones and nutritional status. Key regulatory elements and cognate transcription factors are still being defined.
ACC specific activity is also rapidly modulated, being increased in response to insulin and decreased following exposure of cells to catabolic hormones or environmental stress. The acute control of ACC activity is the product of integrated changes in substrate supply, allosteric ligands, the phosphorylation of multiple serine residues and interactions with other proteins. This review traces the path and implications of studies initiated with Dick Denton in Bristol in the late s, through to current proteomic and other approaches that have been consistently challenging and immensely rewarding.
Sign In or Create an Account. Advanced Search. Sign In. Skip Nav Destination Article Navigation. ACC specific activity is also rapidly modulated, being increased in response to insulin and decreased following exposure of cells to catabolic hormones or environmental stress. The acute control of ACC activity is the product of integrated changes in substrate supply, allosteric ligands, the phosphorylation of multiple serine residues and interactions with other proteins. This review traces the path and implications of studies initiated with Dick Denton in Bristol in the late s, through to current proteomic and other approaches that have been consistently challenging and immensely rewarding.
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