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Noncovalent dimerization of ubiquitin.

Liu Z, Zhang WP, Xing Q, Ren X, Liu M, Tang C - Angew. Chem. Int. Ed. Engl. (2011)

Bottom Line: Another kind of dynamics: Ubiquitin noncovalently dimerizes with a dissociation constant of approximately 5 mM.The two subunits adopt an array of relative orientations, utilizing an interface also for binding to other proteins (see picture).Quaternary fluctuation among members of the dimer ensemble constitutes a different kind of dynamics that complements the tertiary dynamics of each ubiquitin subunit.

View Article: PubMed Central - PubMed

Affiliation: State Key Laboratory of Magnetic Resonance and Atomic and Molecular Physics, Wuhan Institute of Physics and Mathematics, Chinese Academy of Sciences, Wuhan, Hubei 430071, China.

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Comparison between the crystal structure of Lys48-linked di-ubiquitin and the ensemble structure of ubiquitin noncovalent dimer; a) the proximal unit (purple surface) of the di-ubiquitin crystal structure3a is superimposed to one subunit in the ensemble structure of the noncovalent dimer; the distal unit is shown as blue cartoon. The noncovalent dimer is represented the same way as in Figure 3; b) colored in orange, a large portion of the noncovalent dimer interface becomes exposed in Lys48-linked di-ubiquitin. The covalent dimer interface is colored in red.
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fig05: Comparison between the crystal structure of Lys48-linked di-ubiquitin and the ensemble structure of ubiquitin noncovalent dimer; a) the proximal unit (purple surface) of the di-ubiquitin crystal structure3a is superimposed to one subunit in the ensemble structure of the noncovalent dimer; the distal unit is shown as blue cartoon. The noncovalent dimer is represented the same way as in Figure 3; b) colored in orange, a large portion of the noncovalent dimer interface becomes exposed in Lys48-linked di-ubiquitin. The covalent dimer interface is colored in red.

Mentions: Secondly, a covalent linkage may restrict the relative movement for the two adjacent subunits in a poly(ubiquitin), and select a subset of conformers from the ensemble structure of the non-covalent dimer. Indeed, the crystal structure of Lys48-linked di-ubiquitin falls into the boundary of the atomic probability map delineated by the noncovalent dimer (Figure 5a). The noncovalent dimer, however, encompasses more interfacial residues than the Lys-48 linked covalent dimer—residues 4–7, 10–12, and 62–66 that are part of the dimer interface in the former become solvent-exposed in the latter (Figure 5b). Interestingly, these residues are also involved in interactions with certain UBDs20a–d and may permit the initial latching in respective binding processes.


Noncovalent dimerization of ubiquitin.

Liu Z, Zhang WP, Xing Q, Ren X, Liu M, Tang C - Angew. Chem. Int. Ed. Engl. (2011)

Comparison between the crystal structure of Lys48-linked di-ubiquitin and the ensemble structure of ubiquitin noncovalent dimer; a) the proximal unit (purple surface) of the di-ubiquitin crystal structure3a is superimposed to one subunit in the ensemble structure of the noncovalent dimer; the distal unit is shown as blue cartoon. The noncovalent dimer is represented the same way as in Figure 3; b) colored in orange, a large portion of the noncovalent dimer interface becomes exposed in Lys48-linked di-ubiquitin. The covalent dimer interface is colored in red.
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC3303887&req=5

fig05: Comparison between the crystal structure of Lys48-linked di-ubiquitin and the ensemble structure of ubiquitin noncovalent dimer; a) the proximal unit (purple surface) of the di-ubiquitin crystal structure3a is superimposed to one subunit in the ensemble structure of the noncovalent dimer; the distal unit is shown as blue cartoon. The noncovalent dimer is represented the same way as in Figure 3; b) colored in orange, a large portion of the noncovalent dimer interface becomes exposed in Lys48-linked di-ubiquitin. The covalent dimer interface is colored in red.
Mentions: Secondly, a covalent linkage may restrict the relative movement for the two adjacent subunits in a poly(ubiquitin), and select a subset of conformers from the ensemble structure of the non-covalent dimer. Indeed, the crystal structure of Lys48-linked di-ubiquitin falls into the boundary of the atomic probability map delineated by the noncovalent dimer (Figure 5a). The noncovalent dimer, however, encompasses more interfacial residues than the Lys-48 linked covalent dimer—residues 4–7, 10–12, and 62–66 that are part of the dimer interface in the former become solvent-exposed in the latter (Figure 5b). Interestingly, these residues are also involved in interactions with certain UBDs20a–d and may permit the initial latching in respective binding processes.

Bottom Line: Another kind of dynamics: Ubiquitin noncovalently dimerizes with a dissociation constant of approximately 5 mM.The two subunits adopt an array of relative orientations, utilizing an interface also for binding to other proteins (see picture).Quaternary fluctuation among members of the dimer ensemble constitutes a different kind of dynamics that complements the tertiary dynamics of each ubiquitin subunit.

View Article: PubMed Central - PubMed

Affiliation: State Key Laboratory of Magnetic Resonance and Atomic and Molecular Physics, Wuhan Institute of Physics and Mathematics, Chinese Academy of Sciences, Wuhan, Hubei 430071, China.

Show MeSH
Related in: MedlinePlus