3PIN: Crystal Structure Of Mxr1 From Saccharomyces Cerevisiae In Complex With Trx2

Citation:
Abstract
The methionine S-sulfoxide reductase MsrA catalyzes the reduction of methionine sulfoxide, a ubiquitous reaction depending on the thioredoxin system. To investigate interactions between MsrA and thioredoxin (Trx), we determined the crystal structures of yeast MsrA/Mxr1 in their reduced, oxidized, and Trx2-complexed forms, at 2.03, 1.90, and 2.70 A, respectively. Comparative structure analysis revealed significant conformational changes of the three loops, which form a plastic "cushion" to harbor the electron donor Trx2. The flexible C-terminal loop enabled Mxr1 to access the methionine sulfoxide on various protein substrates. Moreover, the plasticity of the Trx binding site on Mxr1 provides structural insights into the recognition of diverse substrates by a universal catalytic motif of Trx.
PDB ID: 3PINDownload
MMDB ID: 88847
PDB Deposition Date: 2010/11/7
Updated in MMDB: 2011/05
Experimental Method:
x-ray diffraction
Resolution: 2.7  Å
Source Organism:
Similar Structures:
Biological Unit for 3PIN: dimeric; determined by author and by software (PISA)
Molecular Components in 3PIN
Label Count Molecule
Proteins (2 molecules)
1
Thioredoxin-2(Gene symbol: TRX2)
Molecule annotation
1
Peptide Methionine Sulfoxide Reductase(Gene symbol: MXR1)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

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