PMID:12032090: Difference between revisions
Table edited by Bmcintosh via TableEdit |
imported>Wikientrybot Fix links due to TableEditLinks.php changes. |
||
| Line 33: | Line 33: | ||
| | | | ||
GO:0003723 | |||
| | | | ||
RNA binding | RNA binding | ||
| Line 52: | Line 52: | ||
| | | | ||
GO:0005524 | |||
| | | | ||
ATP binding | ATP binding | ||
Revision as of 00:38, 20 February 2009
Newberry, KJ, Hou, YM and Perona, JJ (2002) Structural origins of amino acid selection without editing by cysteinyl-tRNA synthetase.EMBO J. 21:2778-87
| Abstract | Cysteinyl-tRNA synthetase (CysRS) is highly specific for synthesis of cysteinyl adenylate, yet does not possess the amino acid editing activity characteristic of many other tRNA synthetases. To elucidate how CysRS is able to distinguish cysteine from non-cognate amino acids, crystal structures of the Escherichia coli enzyme were determined in apo and cysteine-bound states. The structures reveal that the substrate cysteine thiolate forms a single direct interaction with a zinc ion bound at the base of the active site cleft, in a trigonal bipyramidal geometry together with four highly conserved protein side chains. Cysteine binding induces movement of the zinc ion towards substrate, as well as flipping of the conserved Trp205 indole ring to pack on the thiol side chain. The imidazole groups of five conserved histidines lie adjacent to the zinc ion, forming a unique arrangement suggestive of functional significance. Thus, amino acid discrimination without editing arises most directly from the favorable zinc-thiolate interaction, which is not possible for non-cognate substrates. Additional selectivity may be generated during the induced-fit conformational changes that help assemble the active site. |
| Links | PubMed Online version:10.1093/emboj/21.11.2778 |
Significance
You can help EcoliWiki by summarizing why this paper is useful
Useful Materials and Methods
You can help Ecoliwiki by describing the useful materials (strains, plasmids, antibodies, etc) described in this paper.
Annotations
| Gene product | Qualifier | GO ID | GO term name | Evidence Code | with/from | Aspect | Notes | Status |
|---|---|---|---|---|---|---|---|---|
| GO:0003723 |
RNA binding |
IPI: Inferred from Physical Interaction |
F |
tRNA appears to bind to the N-terminal domain of CysRS (Figure 3). |
complete | |||
| GO:0005524 |
ATP binding |
IPI: Inferred from Physical Interaction |
F |
An ATP molecule is predicted to be coordinated by the N-terminal domain of CysS, and soaking of the crystals in the presence of ATP and cysteine decreased the resolution in this region (Figure 6). |
complete | |||
| edit table |
EcoliWiki Links
Add links to pages that link here (e.g. gene, product, method pages)
See also
References
See Help:References for how to manage references in EcoliWiki.