From Proteopedia
(Difference between revisions)
proteopedia linkproteopedia link
|
|
| Line 1: |
Line 1: |
| - | [[Image:1z7y.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:1z7y.png|left|200px]] |
| | | | |
| | <!-- | | <!-- |
| Line 9: |
Line 10: |
| | {{STRUCTURE_1z7y| PDB=1z7y | SCENE= }} | | {{STRUCTURE_1z7y| PDB=1z7y | SCENE= }} |
| | | | |
| - | '''Crystal Structure of the Arabidopsis thaliana O-Acetylserine Sulfhydrylase K46A mutant'''
| + | ===Crystal Structure of the Arabidopsis thaliana O-Acetylserine Sulfhydrylase K46A mutant=== |
| | | | |
| | | | |
| - | ==Overview==
| + | <!-- |
| - | In plants, cysteine biosynthesis plays a central role in fixing inorganic sulfur from the environment and provides the only metabolic sulfide donor for the generation of methionine, glutathione, phytochelatins, iron-sulfur clusters, vitamin cofactors, and multiple secondary metabolites. O-Acetylserine sulfhydrylase (OASS) catalyzes the final step of cysteine biosynthesis, the pyridoxal 5'-phosphate (PLP)-dependent conversion of O-acetylserine into cysteine. Here we describe the 2.2 A resolution crystal structure of OASS from Arabidopsis thaliana (AtOASS) and the 2.7 A resolution structure of the AtOASS K46A mutant with PLP and methionine covalently linked as an external aldimine in the active site. Although the plant and bacterial OASS share a conserved set of amino acids for PLP binding, the structure of AtOASS reveals a difference from the bacterial enzyme in the positioning of an active site loop formed by residues 74-78 when methionine is bound. Site-directed mutagenesis, kinetic analysis, and ligand binding titrations probed the functional roles of active site residues. These experiments indicate that Asn(77) and Gln(147) are key amino acids for O-acetylserine binding and that Thr(74) and Ser(75) are involved in sulfur incorporation into cysteine. In addition, examination of the AtOASS structure and nearly 300 plant and bacterial OASS sequences suggest that the highly conserved beta8A-beta9A surface loop may be important for interaction with serine acetyltransferase, the other enzyme in cysteine biosynthesis. Initial protein-protein interaction experiments using AtOASS mutants targeted to this loop support this hypothesis.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_16166087}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 16166087 is the PubMed ID number. |
| | + | --> |
| | + | {{ABSTRACT_PUBMED_16166087}} |
| | | | |
| | ==About this Structure== | | ==About this Structure== |
| Line 28: |
Line 32: |
| | [[Category: Knapke, S M.]] | | [[Category: Knapke, S M.]] |
| | [[Category: Transferase]] | | [[Category: Transferase]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 17:17:25 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 08:51:20 2008'' |
Revision as of 05:51, 28 July 2008
Template:STRUCTURE 1z7y
Crystal Structure of the Arabidopsis thaliana O-Acetylserine Sulfhydrylase K46A mutant
Template:ABSTRACT PUBMED 16166087
About this Structure
1Z7Y is a Single protein structure of sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA.
Reference
Molecular basis of cysteine biosynthesis in plants: structural and functional analysis of O-acetylserine sulfhydrylase from Arabidopsis thaliana., Bonner ER, Cahoon RE, Knapke SM, Jez JM, J Biol Chem. 2005 Nov 18;280(46):38803-13. Epub 2005 Sep 15. PMID:16166087
Page seeded by OCA on Mon Jul 28 08:51:20 2008
