2K7K
Human Acylphosphatase (AcPh) common type
Summary for 2K7K
| Entry DOI | 10.2210/pdb2k7k/pdb |
| Related | 2k7j |
| Descriptor | Acylphosphatase-1 (1 entity in total) |
| Functional Keywords | protein, acetylation, hydrolase |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 1 |
| Total formula weight | 11203.70 |
| Authors | Gribenko, A.V.,Patel, M.M.,Liu, J.,McCallum, S.A.,Wang, C.,Makhatadze, G.I. (deposition date: 2008-08-13, release date: 2009-02-17, Last modification date: 2024-05-22) |
| Primary citation | Gribenko, A.V.,Patel, M.M.,Liu, J.,McCallum, S.A.,Wang, C.,Makhatadze, G.I. Rational stabilization of enzymes by computational redesign of surface charge-charge interactions Proc.Natl.Acad.Sci.USA, 106:2601-2606, 2009 Cited by PubMed Abstract: Here, we report the application of a computational approach that allows the rational design of enzymes with enhanced thermostability while retaining full enzymatic activity. The approach is based on the optimization of the energy of charge-charge interactions on the protein surface. We experimentally tested the validity of the approach on 2 human enzymes, acylphosphatase (AcPh) and Cdc42 GTPase, that differ in size (98 vs. 198-aa residues, respectively) and tertiary structure. We show that the designed proteins are significantly more stable than the corresponding WT proteins. The increase in stability is not accompanied by significant changes in structure, oligomerization state, or, most importantly, activity of the designed AcPh or Cdc42. This success of the design methodology suggests that it can be universally applied to other enzymes, on its own or in combination with the other strategies based on redesign of the interactions in the protein core. PubMed: 19196981DOI: 10.1073/pnas.0808220106 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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