Abstract
Myosin light-chain kinase is responsible for the phosphorylation of myosin in smooth muscle cells. In some tissue types, the C-terminal portion of this large enzyme is expressed as an independent protein and has been given the name telokin. Recently, an antibody directed against telokin was found to interact with a protein derived from the baculovirus Autographa californica nuclear polyhedrosis virus. This protein was biochemically characterized and given the name TLP20 for telokin-like protein of 20 000 molecular weight. The amino-acid sequence of TLP20 was determined on the basis of a cDNA clone and subsequent alignment searches failed to reveal any homology to telokin or to other known proteins. The three-dimensional structure of a proteolytic portion of TLP20 is reported here. Crystals employed in the investigation were grown from ammonium sulfate solutions at pH 6.0 and belonged to the space group P213 with unit-cell dimensions of a = b = c = 76.3 Å and one molecule per asymmetric unit. The structure was determined by multiple isomorphous replacement with three heavy-atom derivatives. Least-squares refinement of the model reduced the crystallographic R factor to 18.1% for all measured X-ray data from 30.0 to 2.2 Å. The overall fold of the molecule may be described as a seven-stranded antiparallel β-barrel flanked on the bottom by two additional β-strands and on top by an α-helix. Quite surprisingly, the three-dimensional structure of this β-barrel is not similar to telokin or to any other known protein.
Original language | English (US) |
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Pages (from-to) | 1153-1160 |
Number of pages | 8 |
Journal | Acta Crystallographica Section D: Biological Crystallography |
Volume | 52 |
Issue number | 6 |
DOIs | |
State | Published - 1996 |
ASJC Scopus subject areas
- Structural Biology
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STRUCTURE OF TLP20
Holden, H. M. (Contributor), Wesenberg, G. (Contributor), Raynes, D. A. (Contributor), Hartshorne, D. J. (Contributor), Guerriero Jr., V. (Contributor) & Rayment, I. (Contributor), Protein Data Bank (PDB), Feb 17 1997
DOI: 10.2210/pdb1TUL/pdb, https://www.wwpdb.org/pdb?id=pdb_00001tul
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