1tul
From Proteopedia
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STRUCTURE OF TLP20
Overview
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 P2(1)3 with unit-cell dimensions, of a = b = c = 76.3 A 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 A. The overall fold of the molecule may be described as a, seven-stranded antiparallel beta-barrel flanked on the bottom by two, additional beta-strands and on the top by an alpha-helix. Quite, surprisingly, the three-dimensional structure of this beta-barrel is not, similar to telokin or to any other known protein.
About this Structure
1TUL is a Single protein structure of sequence from Autographa californica nucleopolyhedrovirus. Full crystallographic information is available from OCA.
Reference
Molecular structure of a proteolytic fragment of TLP20., Holden HM, Wesenberg G, Raynes DA, Hartshorne DJ, Guerriero V Jr, Rayment I, Acta Crystallogr D Biol Crystallogr. 1996 Nov 1;52(Pt 6):1153-60. PMID:15299576
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