1m9l
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:1m9l.gif|left|200px]] | [[Image:1m9l.gif|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_1m9l", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | | | + | or leave the SCENE parameter empty for the default display. |
| - | | | + | --> |
| - | + | {{STRUCTURE_1m9l| PDB=1m9l | SCENE= }} | |
| - | + | ||
| - | + | ||
| - | }} | + | |
'''Relaxation-based Refined Structure Of Chlamydomonas Outer Arm Dynein Light Chain 1''' | '''Relaxation-based Refined Structure Of Chlamydomonas Outer Arm Dynein Light Chain 1''' | ||
| Line 31: | Line 28: | ||
[[Category: Mullen, G P.]] | [[Category: Mullen, G P.]] | ||
[[Category: Wu, H W.]] | [[Category: Wu, H W.]] | ||
| - | [[Category: | + | [[Category: Backbone dynamic]] |
| - | [[Category: | + | [[Category: Leucine-rich repeat]] |
| - | [[Category: | + | [[Category: Relaxation]] |
| - | [[Category: | + | [[Category: Structural refinement]] |
| - | [[Category: | + | [[Category: Structure from molmol]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:47:43 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 21:47, 2 May 2008
Relaxation-based Refined Structure Of Chlamydomonas Outer Arm Dynein Light Chain 1
Overview
The light chain 1 (LC1) polypeptide is a member of the leucine-rich repeat protein family and binds at or near the ATP hydrolytic site within the motor domain of the gamma heavy chain from Chlamydomonas outer arm dynein. It consists of an N-terminal helix, a central barrel formed from six leucine-rich repeats that fold as beta beta alpha units, and a C-terminal helical domain that protrudes from the main axis defined by the leucine-rich repeats. Interaction with the gamma heavy chain is likely mediated through a hydrophobic patch on the larger beta sheet face, and the C-terminal region is predicted to insert into the dynein ATP hydrolytic site. Here we have used 1H-15N heteronuclear relaxation measurements obtained at 500 and 600 MHz to refine and validate the LC1 solution structure. In this refined structure, the C-terminal helix is significantly reoriented by more than 20 degrees as compared to the control and provides a more precise understanding of the potential regulatory role of this domain. We also employed the refined structure to perform a dynamic analysis of LC1 using the 600 MHz data set. These results, which were cross validated using the 500 MHz data set, strongly support identification of the predicted LC1 binding surfaces and provide additional insight into the interaction mechanisms of leucine-rich repeat proteins.
About this Structure
1M9L is a Single protein structure of sequence from Chlamydomonas reinhardtii. Full crystallographic information is available from OCA.
Reference
Relaxation-based structure refinement and backbone molecular dynamics of the dynein motor domain-associated light chain., Wu H, Blackledge M, Maciejewski MW, Mullen GP, King SM, Biochemistry. 2003 Jan 14;42(1):57-71. PMID:12515539 Page seeded by OCA on Sat May 3 00:47:43 2008
