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[[Image:1ds9.jpg|left|200px]]
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{{STRUCTURE_1ds9|  PDB=1ds9  |  SCENE=  }}
'''SOLUTION STRUCTURE OF CHLAMYDOMONAS OUTER ARM DYNEIN LIGHT CHAIN 1'''


==SOLUTION STRUCTURE OF CHLAMYDOMONAS OUTER ARM DYNEIN LIGHT CHAIN 1==
<StructureSection load='1ds9' size='340' side='right'caption='[[1ds9]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1ds9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Chlamydomonas_reinhardtii Chlamydomonas reinhardtii]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DS9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DS9 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ds9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ds9 OCA], [https://pdbe.org/1ds9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ds9 RCSB], [https://www.ebi.ac.uk/pdbsum/1ds9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ds9 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/DNAL1_CHLRE DNAL1_CHLRE] Associates with the gamma heavy chain in the outer arm dynein. May target p45 polypeptide (an 45 kDa axonemal component) to the motor domain of the gamma heavy chain dynein.<ref>PMID:10353837</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ds/1ds9_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ds9 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


==Overview==
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<ref>PMID:10876244</ref>
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==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1DS9 is a [[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].
</div>
<div class="pdbe-citations 1ds9" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
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:[http://www.ncbi.nlm.nih.gov/pubmed/10876244 10876244]
*[[Dynein 3D structures|Dynein 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Chlamydomonas reinhardtii]]
[[Category: Chlamydomonas reinhardtii]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Benashski, S E.]]
[[Category: Benashski SE]]
[[Category: King, S M.]]
[[Category: King SM]]
[[Category: Maciejewski, M W.]]
[[Category: Maciejewski MW]]
[[Category: Marintchev, A.]]
[[Category: Marintchev A]]
[[Category: Mullen, G P.]]
[[Category: Mullen GP]]
[[Category: Wu, H W.]]
[[Category: Wu HW]]
[[Category: Beta-beta-alpha cylinder]]
[[Category: Chlamydomona]]
[[Category: Dynein]]
[[Category: Flagella]]
[[Category: Leucine-rich repeat]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 14:12:48 2008''

Latest revision as of 08:25, 22 May 2024

SOLUTION STRUCTURE OF CHLAMYDOMONAS OUTER ARM DYNEIN LIGHT CHAIN 1

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