1ds9

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(New page: 200px<br /><applet load="1ds9" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ds9" /> '''SOLUTION STRUCTURE OF CHLAMYDOMONAS OUTER AR...)
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[[Image:1ds9.jpg|left|200px]]<br /><applet load="1ds9" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1ds9" />
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'''SOLUTION STRUCTURE OF CHLAMYDOMONAS OUTER ARM DYNEIN LIGHT CHAIN 1'''<br />
'''SOLUTION STRUCTURE OF CHLAMYDOMONAS OUTER ARM DYNEIN LIGHT CHAIN 1'''<br />
==Overview==
==Overview==
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Dyneins are molecular motors that translocate towards the minus ends of, microtubules. In Chlamydomonas flagellar outer arm dynein, light chain 1, (LC1) associates with the nucleotide binding region within the gamma heavy, chain motor domain and consists of a central leucine-rich repeat section, that folds as a cylindrical right handed spiral formed from six, beta-beta-alpha motifs. This central cylinder is flanked by terminal, helical subdomains. The C-terminal helical domain juts out from the, cylinder and is adjacent to a hydrophobic surface within the repeat region, that is proposed to interact with the dynein heavy chain. The position of, the C-terminal domain on LC1 and the unexpected structural similarity, between LC1 and U2A' from the human spliceosome suggest that this domain, interacts with the dynein motor domain.
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Dyneins are molecular motors that translocate towards the minus ends of microtubules. In Chlamydomonas flagellar outer arm dynein, light chain 1 (LC1) associates with the nucleotide binding region within the gamma heavy chain motor domain and consists of a central leucine-rich repeat section that folds as a cylindrical right handed spiral formed from six beta-beta-alpha motifs. This central cylinder is flanked by terminal helical subdomains. The C-terminal helical domain juts out from the cylinder and is adjacent to a hydrophobic surface within the repeat region that is proposed to interact with the dynein heavy chain. The position of the C-terminal domain on LC1 and the unexpected structural similarity between LC1 and U2A' from the human spliceosome suggest that this domain interacts with the dynein motor domain.
==About this Structure==
==About this Structure==
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1DS9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Chlamydomonas_reinhardtii Chlamydomonas reinhardtii]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DS9 OCA].
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1DS9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Chlamydomonas_reinhardtii Chlamydomonas reinhardtii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DS9 OCA].
==Reference==
==Reference==
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[[Category: Chlamydomonas reinhardtii]]
[[Category: Chlamydomonas reinhardtii]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Benashski, S.E.]]
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[[Category: Benashski, S E.]]
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[[Category: King, S.M.]]
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[[Category: King, S M.]]
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[[Category: Maciejewski, M.W.]]
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[[Category: Maciejewski, M W.]]
[[Category: Marintchev, A.]]
[[Category: Marintchev, A.]]
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[[Category: Mullen, G.P.]]
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[[Category: Mullen, G P.]]
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[[Category: Wu, H.W.]]
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[[Category: Wu, H W.]]
[[Category: beta-beta-alpha cylinder]]
[[Category: beta-beta-alpha cylinder]]
[[Category: chlamydomonas]]
[[Category: chlamydomonas]]
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[[Category: leucine-rich repeat]]
[[Category: leucine-rich repeat]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:32:41 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:19:54 2008''

Revision as of 10:19, 21 February 2008


1ds9

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SOLUTION STRUCTURE OF CHLAMYDOMONAS OUTER ARM DYNEIN LIGHT CHAIN 1

Overview

Dyneins are molecular motors that translocate towards the minus ends of microtubules. In Chlamydomonas flagellar outer arm dynein, light chain 1 (LC1) associates with the nucleotide binding region within the gamma heavy chain motor domain and consists of a central leucine-rich repeat section that folds as a cylindrical right handed spiral formed from six beta-beta-alpha motifs. This central cylinder is flanked by terminal helical subdomains. The C-terminal helical domain juts out from the cylinder and is adjacent to a hydrophobic surface within the repeat region that is proposed to interact with the dynein heavy chain. The position of the C-terminal domain on LC1 and the unexpected structural similarity between LC1 and U2A' from the human spliceosome suggest that this domain interacts with the dynein motor domain.

About this Structure

1DS9 is a Single protein structure of sequence from Chlamydomonas reinhardtii. Full crystallographic information is available from OCA.

Reference

Solution structure of a dynein motor domain associated light chain., Wu H, Maciejewski MW, Marintchev A, Benashski SE, Mullen GP, King SM, Nat Struct Biol. 2000 Jul;7(7):575-9. PMID:10876244

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