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Atomic-Resolution Structures of the APC/C Subunits Apc4 and the Apc5 N-Terminal Domain.

Cronin NB, Yang J, Zhang Z, Kulkarni K, Chang L, Yamano H, Barford D - J. Mol. Biol. (2015)

Bottom Line: Apc4 comprises a WD40 domain split by a long α-helical domain, whereas Apc5(N) has an α-helical fold.In a separate study, we had fitted these atomic models to a 3.6-Å-resolution cryo-electron microscopy map of the APC/C.We discuss the complementary approaches of high-resolution electron microscopy and protein crystallography to the structure determination of subunits of multimeric complexes.

View Article: PubMed Central - PubMed

Affiliation: Division of Structural Biology, Institute of Cancer Research, 237 Fulham Road, London SW3 6JB, United Kingdom.

No MeSH data available.


Related in: MedlinePlus

Comparison of EM density maps of APC/CCdh1.Emi1 and crystal structure 2Fo − Fc maps of human Apc4HBD. (a) Stereoview of the EM density map and Apc4 coordinates. Main chain is shown as a cartoon, and amino acid side chains are shown as sticks. (b) Stereoview of the 2Fo − Fc density map contoured at 1σ and Apc4 coordinates. Main chain is shown as a cartoon, and amino acid side chains are shown as sticks.
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f0025: Comparison of EM density maps of APC/CCdh1.Emi1 and crystal structure 2Fo − Fc maps of human Apc4HBD. (a) Stereoview of the EM density map and Apc4 coordinates. Main chain is shown as a cartoon, and amino acid side chains are shown as sticks. (b) Stereoview of the 2Fo − Fc density map contoured at 1σ and Apc4 coordinates. Main chain is shown as a cartoon, and amino acid side chains are shown as sticks.

Mentions: Figure 3 shows a comparison of the EM density and X-ray (2Fo − Fc) maps of human Apc4, determined to similar resolutions, 3.6 Å and 3.4 Å, respectively. In the EM density map, secondary structural features are well defined, whereas secondary structural elements at the tip and periphery of Apc4HBD that are resolved in the EM density map are disordered in the X-ray structure (α4, α9 and α10). For both EM and X-ray maps, within the core of Apc4HBD, amino acid side-chain densities are of comparable quality, allowing ab initio fitting of the polypeptide sequence (Fig. 4).


Atomic-Resolution Structures of the APC/C Subunits Apc4 and the Apc5 N-Terminal Domain.

Cronin NB, Yang J, Zhang Z, Kulkarni K, Chang L, Yamano H, Barford D - J. Mol. Biol. (2015)

Comparison of EM density maps of APC/CCdh1.Emi1 and crystal structure 2Fo − Fc maps of human Apc4HBD. (a) Stereoview of the EM density map and Apc4 coordinates. Main chain is shown as a cartoon, and amino acid side chains are shown as sticks. (b) Stereoview of the 2Fo − Fc density map contoured at 1σ and Apc4 coordinates. Main chain is shown as a cartoon, and amino acid side chains are shown as sticks.
© Copyright Policy - CC BY
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4590430&req=5

f0025: Comparison of EM density maps of APC/CCdh1.Emi1 and crystal structure 2Fo − Fc maps of human Apc4HBD. (a) Stereoview of the EM density map and Apc4 coordinates. Main chain is shown as a cartoon, and amino acid side chains are shown as sticks. (b) Stereoview of the 2Fo − Fc density map contoured at 1σ and Apc4 coordinates. Main chain is shown as a cartoon, and amino acid side chains are shown as sticks.
Mentions: Figure 3 shows a comparison of the EM density and X-ray (2Fo − Fc) maps of human Apc4, determined to similar resolutions, 3.6 Å and 3.4 Å, respectively. In the EM density map, secondary structural features are well defined, whereas secondary structural elements at the tip and periphery of Apc4HBD that are resolved in the EM density map are disordered in the X-ray structure (α4, α9 and α10). For both EM and X-ray maps, within the core of Apc4HBD, amino acid side-chain densities are of comparable quality, allowing ab initio fitting of the polypeptide sequence (Fig. 4).

Bottom Line: Apc4 comprises a WD40 domain split by a long α-helical domain, whereas Apc5(N) has an α-helical fold.In a separate study, we had fitted these atomic models to a 3.6-Å-resolution cryo-electron microscopy map of the APC/C.We discuss the complementary approaches of high-resolution electron microscopy and protein crystallography to the structure determination of subunits of multimeric complexes.

View Article: PubMed Central - PubMed

Affiliation: Division of Structural Biology, Institute of Cancer Research, 237 Fulham Road, London SW3 6JB, United Kingdom.

No MeSH data available.


Related in: MedlinePlus