PDBsum entry 1ds9

Contractile protein

PDB id: 1ds9

Contents

Protein chain

198 a.a. *

* Residue conservation analysis

PDB id:

1ds9

Name:

Contractile protein

Title:

Solution structure of chlamydomonas outer arm dynein light chain 1

Structure:

Outer arm dynein. Chain: a. Fragment: light chain 1. Engineered: yes

Source:

Chlamydomonas reinhardtii. Organism_taxid: 3055. Organ: flagellae. Expressed in: escherichia coli. Expression_system_taxid: 562.

NMR struc:

17 models

Authors:

H.W.Wu,M.W.Maciejewski,A.Marintchev,S.E.Benashski,G.P.Mullen,S.M.King

Key ref:

H.Wu et al. (2000). Solution structure of a dynein motor domain associated light chain. Nat Struct Biol, 7, 575-579. PubMed id: 10876244 DOI: 10.1038/76804

Date:

07-Jan-00 Release date: 26-Jul-00

Protein chain

Q9XHH2  (DNAL1_CHLRE) -  Dynein axonemal light chain 1 from Chlamydomonas reinhardtii

Seq: 198 a.a.

Struc: 198 a.a.

DOI no: 10.1038/76804

Nat Struct Biol 7:575-579 (2000)

PubMed id: 10876244

Solution structure of a dynein motor domain associated light chain.

H.Wu, M.W.Maciejewski, A.Marintchev, S.E.Benashski, G.P.Mullen, S.M.King.

ABSTRACT

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.

Selected figure(s)

Figure 2.
Figure 2. The NMR solution structure of LC1. a, Stereo view of the backbone trace for a superposition of the 17 lowest energy LC1 structures is shown. Colors used for the -helices and -strands correspond to the topology diagram in Fig. 1b. The N-terminus is at the bottom of the displayed structures. b, Ribbon representation of the mean LC1 structure with individual secondary structure elements labeled. c, Superimposition of the hydrophobic side chains (green) that pack the core of the leucine rich repeat region are shown on the mean backbone (orange).

Figure 3.
Figure 3. Electrostatic surface of LC1 and proposed heavy chain binding site. a, Two views (related by 90° rotation about the y-axis) of the electrostatic surface of LC1 are shown. The hydrophobic patch, which includes Trp 99, Tyr 121 and Leu 146 on the -sheet face, is evident in the view on the right. It is this patch that may be involved in attachment of LC1 to the heavy chain. The opposite surface proposed to interact with p45 (left view) is highly charged, with patches of both acidic and basic residues. The surface potential was calculated using dielectric constants of 30 and 80 for protein and solvent, respectively. The images are oriented with the N-terminus to the top. b, Close up stereo view of the putative heavy chain binding surface. Side chains at positions that are hydrophobic in all family members are shown in green (Trp 99 and Leu 146), whereas hydrophobic side chains at less conserved positions are in yellow (Ile 74, Tyr 102, Val 119 and Tyr 121). Acidic and basic residues that surround the hydrophobic patch are shown in red and blue, respectively. c, The superimposed ribbon structures of LC1 (orange) and U2A' (yellow; accession code 1A9N) are shown to illustrate the structural homology between these two molecules. The r.m.s. deviation for superimposed C atoms is 3.7 Å as determined by DALI (version 2.0)30.

The above figures are reprinted by permission from Macmillan Publishers Ltd: Nat Struct Biol (2000, 7, 575-579) copyright 2000.

Figures were selected by the author.