The structure ofStaphylococcus aureusphosphopantetheine adenylyltransferase in complex with 3′-phosphoadenosine 5′-phosphosulfate reveals a new ligand-binding mode
| Autor: | Ji Yong Kang, Ji Hyeon Park, Kwang Hyun Choi, Seung Kyu Lee, Hyung Ho Lee, Se Won Suh, Jin-Su Song, Hye-Jin Yoon, Dojin Kim, Hie Joon Kim |
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| Rok vydání: | 2009 |
| Předmět: |
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Molecular Staphylococcus aureus Stereochemistry Coenzyme A Molecular Sequence Data Phosphoadenosine Phosphosulfate Biophysics Sequence alignment Biology Crystallography X-Ray Biochemistry Pyrophosphate chemistry.chemical_compound Structural Biology Genetics Structural Communications Transferase Amino Acid Sequence Binding site Protein Structure Quaternary Peptide sequence Condensed Matter Physics Nucleotidyltransferase Nucleotidyltransferases 3'-Phosphoadenosine-5'-phosphosulfate chemistry Sequence Alignment |
| Zdroj: | Acta Crystallographica Section F Structural Biology and Crystallization Communications. 65:987-991 |
| ISSN: | 1744-3091 |
| Popis: | Bacterial phosphopantetheine adenylyltransferase (PPAT) catalyzes the penultimate step in the coenzyme A (CoA) biosynthetic pathway. It catalyzes the reversible transfer of an adenylyl group from ATP to 4′-phosphopantetheine (Ppant) to form dephospho-CoA (dPCoA) and pyrophosphate. Previous structural studies have revealed how several ligands are recognized by bacterial PPATs. ATP, ADP, Ppant and dPCoA bind to the same binding site in a highly similar manner, while CoA binds to a partially overlapping site in a different mode. To provide further structural insights into ligand binding, the crystal structure of Staphylococcus aureus PPAT was solved in a binary complex with 3′-phosphoadenosine 5′-phosphosulfate (PAPS). This study unexpectedly revealed a new mode of ligand binding to PPAT, thus providing potentially useful information for structure-based discovery of inhibitors of bacterial PPATs. |
| Databáze: | OpenAIRE |
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