| Autor: |
Stauffer ME; School of Molecular Biosciences, Washington State University, Pullman, WA 99164-4660, USA., Young JK, Helms GL, Evans JN |
| Jazyk: |
angličtina |
| Zdroj: |
FEBS letters [FEBS Lett] 2001 Jun 15; Vol. 499 (1-2), pp. 182-6. |
| DOI: |
10.1016/s0014-5793(01)02555-8 |
| Abstrakt: |
To facilitate evaluation of enzyme-ligand complexes in solution, we have isolated the 26-kDa N-terminal domain of 5-enolpyruvylshikimate-3-phosphate (EPSP) synthase for analysis by NMR spectroscopy. The isolated domain is capable of binding the substrate shikimate-3-phosphate (S3P), and this letter reports the localization of the S3P binding site using chemical shift mapping. Based on the NMR data, we propose that Ser23, Arg27, Ser197, and Tyr200 are directly involved in S3P binding. We also describe changes in the observed nuclear Overhauser effects (NOEs) that are consistent with a partial conformational change in the N-terminal domain upon S3P binding. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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