Acetylation of Surface Lysine Groups of a Protein Alters the Organization and Composition of Its Crystal Contacts

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Acetylation of Surface Lysine Groups of a Protein Alters the Organization and Composition of Its Crystal Contacts

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Title: Acetylation of Surface Lysine Groups of a Protein Alters the Organization and Composition of Its Crystal Contacts
Author: Kang, Kyungtae; Choi, Jeong-Mo; Fox, Jerome M.; Snyder, Phillip W.; Moustakas, Demetri T.; Whitesides, George McClelland

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Citation: Kang, Kyungtae, Jeong-Mo Choi, Jerome M. Fox, Phillip W. Snyder, Demetri T. Moustakas, and George M. Whitesides. 2016. Acetylation of Surface Lysine Groups of a Protein Alters the Organization and Composition of Its Crystal Contacts. The Journal of Physical Chemistry B 120, no. 27: 6461–6468. doi:10.1021/acs.jpcb.6b01105.
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Abstract: This paper uses crystals of bovine carbonic anhydrase (CA) and its acetylated variant to examine (i) how a large negative formal charge can be accommodated in protein-protein interfaces, (ii) why lysine residues are often excluded from them, and (iii) how changes in the surface charge of a protein can alter the structure and organization of protein-protein interfaces. It demonstrates that acetylation of lysine residues on the surface of CA increases the participation of polar residues (particularly acetylated lysine) in protein-protein interfaces, and decreases the participation of nonpolar residues in those interfaces. Negatively charged residues are accommodated in protein-protein interfaces via (i) hydrogen bonds or van der Waals interactions with polar residues or (ii) salt bridges with other charged residues. The participation of acetylated lysine in protein-protein interfaces suggests that unacetylated lysine tends to be excluded from interfaces because of its positive charge, and not because of a loss in conformational entropy. Results also indicate that crystal contacts in acetylated CA become less constrained geometrically and, as a result, more closely packed (i.e., more tightly clustered spatially) than those of native CA. This study demonstrates a physical-organic approach—and a well-defined model system—for studying the role of charges in protein-protein interactions.
Published Version: 10.1021/acs.jpcb.6b01105
Terms of Use: This article is made available under the terms and conditions applicable to Open Access Policy Articles, as set forth at http://nrs.harvard.edu/urn-3:HUL.InstRepos:dash.current.terms-of-use#OAP
Citable link to this page: http://nrs.harvard.edu/urn-3:HUL.InstRepos:29954441
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