1tul
From Proteopedia
(New page: 200px<br /><applet load="1tul" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tul, resolution 2.2Å" /> '''STRUCTURE OF TLP20'''...) |
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| - | [[Image:1tul.gif|left|200px]]<br /><applet load="1tul" size=" | + | [[Image:1tul.gif|left|200px]]<br /><applet load="1tul" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1tul, resolution 2.2Å" /> | caption="1tul, resolution 2.2Å" /> | ||
'''STRUCTURE OF TLP20'''<br /> | '''STRUCTURE OF TLP20'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Myosin light-chain kinase is responsible for the phosphorylation of myosin | + | 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== | ==About this Structure== | ||
| - | 1TUL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Autographa_californica_nucleopolyhedrovirus Autographa californica nucleopolyhedrovirus]. Full crystallographic information is available from [http:// | + | 1TUL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Autographa_californica_nucleopolyhedrovirus Autographa californica nucleopolyhedrovirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TUL OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Autographa californica nucleopolyhedrovirus]] | [[Category: Autographa californica nucleopolyhedrovirus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Holden, H | + | [[Category: Holden, H M.]] |
[[Category: Rayment, I.]] | [[Category: Rayment, I.]] | ||
[[Category: telokin-like protein]] | [[Category: telokin-like protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:17:34 2008'' |
Revision as of 13:17, 21 February 2008
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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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