Control of protein oligomerization symmetry by metal coordination: C 2 and C 3 symmetrical assemblies through Cu II and Ni II coordination

Inorganic Chemistry

Volumn 48, Issue 7, 2009, Pages 2726-2728

  Salgado, Eric N ^a,b   Lewis, Richard A ^a,b   Mossin, Susanne ^a,b   Rheingold, Arnold L ^a,b   Tezcan, F Akif ^a,b  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b UNIVERSITY OF ERLANGEN NUREMBERG   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

COPPER; METALLOPROTEIN; NICKEL; ORGANOMETALLIC COMPOUND; ZINC;

ARTICLE; CHEMICAL STRUCTURE; CHEMISTRY; PROTEIN MULTIMERIZATION; PROTEIN QUATERNARY STRUCTURE; SYNTHESIS; X RAY CRYSTALLOGRAPHY;

COPPER; CRYSTALLOGRAPHY, X-RAY; METALLOPROTEINS; MODELS, MOLECULAR; NICKEL; ORGANOMETALLIC COMPOUNDS; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, QUATERNARY; ZINC;

EID: 64349084476     PISSN: 00201669     EISSN: None     Source Type: Journal    
DOI: 10.1021/ic9001237     Document Type: Article

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10. 2.
11. 3, the solvation free-energy gain upon monomer-monomer docking is similarly small (-1.9 kcal/ mol), with a corresponding CSS of zero (Table S6 in the Supporting Information). These findings suggest that oligomerization of MBPC-1 in both structures is driven by metal coordination.
12. In addition, there is a weakly bound Ni ion near the N terminus of each monomer (Figure S6 in the Supporting Information). This Ni ion is internally coordinated to the N-terminal amine and the carbonyl oxygen of Alal, Asp39, and Lys42; it is not involved in any interprotein interactions.
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