2K7V
Deletions in a surface loop divert the folding of a protein domain into a metastable dimeric form
Summary for 2K7V
| Entry DOI | 10.2210/pdb2k7v/pdb |
| NMR Information | BMRB: 15931 |
| Descriptor | Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex (1 entity in total) |
| Functional Keywords | misfolded dimer, acyltransferase, glycolysis, lipoyl, transferase |
| Biological source | Escherichia coli |
| Total number of polymer chains | 2 |
| Total formula weight | 17774.65 |
| Authors | Stott, K.M.,Yusof, A.M.,Perham, R.N.,Jones, D.D. (deposition date: 2008-08-27, release date: 2009-09-15, Last modification date: 2023-06-14) |
| Primary citation | Stott, K.M.,Yusof, A.M.,Perham, R.N.,Jones, D.D. A surface loop directs conformational switching of a lipoyl domain between a folded and a novel misfolded structure. Structure, 17:1117-1127, 2009 Cited by PubMed: 19679089DOI: 10.1016/j.str.2009.07.001 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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