4PLQ
Crystal Structures of Designed Armadillo Repeat Proteins: Implications of Construct Design and Crystallization Conditions on Overall Structure.
Summary for 4PLQ
| Entry DOI | 10.2210/pdb4plq/pdb |
| Descriptor | Arm00011 (2 entities in total) |
| Functional Keywords | peptide binding protein, designed armadillo repeat protein, protein engineering |
| Biological source | synthetic construct |
| Total number of polymer chains | 1 |
| Total formula weight | 29645.01 |
| Authors | Mittl, P.R.,Reichen, C.,Madhurantakam, C.,Pluckthun, A. (deposition date: 2014-05-19, release date: 2014-08-27, Last modification date: 2023-12-20) |
| Primary citation | Reichen, C.,Madhurantakam, C.,Pluckthun, A.,Mittl, P.R. Crystal structures of designed armadillo repeat proteins: Implications of construct design and crystallization conditions on overall structure. Protein Sci., 23:1572-1583, 2014 Cited by PubMed Abstract: Designed armadillo repeat proteins (dArmRP) are promising modular proteins for the engineering of binding molecules that recognize extended polypeptide chains. We determined the structure of a dArmRP containing five internal repeats and 3rd generation capping repeats in three different states by X-ray crystallography: without N-terminal His6 -tag and in the presence of calcium (YM5 A/Ca(2+) ), without N-terminal His6 -tag and in the absence of calcium (YM5 A), and with N-terminal His6 -tag and in the presence of calcium (His-YM5 A/Ca(2+)). All structures show different quaternary structures and superhelical parameters. His-YM5 A/Ca(2+) forms a crystallographic dimer, which is bridged by the His6 -tag, YM5 A/Ca(2+) forms a domain-swapped tetramer, and only in the absence of calcium and the His6 -tag, YM5 A forms a monomer. The changes of superhelical parameters are a consequence of calcium binding, because calcium ions interact with negatively charged residues, which can also participate in the modulation of helix dipole moments between adjacent repeats. These observations are important for further optimizations of dArmRPs and provide a general illustration of how construct design and crystallization conditions can influence the exact structure of the investigated protein. PubMed: 25132085DOI: 10.1002/pro.2535 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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