Acetylation of Surface Lysine Groups of a Protein Alters the Organization and Composition of Its Crystal Contacts
Fox, Jerome M.
Snyder, Phillip W.
Moustakas, Demetri T.
MetadataShow full item record
CitationKang, 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.
AbstractThis 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.
Citable link to this pagehttp://nrs.harvard.edu/urn-3:HUL.InstRepos:29954441
- FAS Scholarly Articles