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| {{STRUCTURE_1gn8| PDB=1gn8 | SCENE= }} | | {{STRUCTURE_1gn8| PDB=1gn8 | SCENE= }} |
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| '''PHOSPHOPANTETHEINE ADENYLYLTRANSFERASE IN COMPLEX WITH MN2+ ATP FROM ESCHERICHIA COLI'''
| | ===PHOSPHOPANTETHEINE ADENYLYLTRANSFERASE IN COMPLEX WITH MN2+ ATP FROM ESCHERICHIA COLI=== |
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| ==Overview==
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| Phosphopantetheine adenylyltransferase (PPAT) is an essential enzyme in the coenzyme A pathway that catalyzes the reversible transfer of an adenylyl group from ATP to 4'-phosphopantetheine (Ppant) in the presence of magnesium. To investigate the reaction mechanism, the high-resolution crystal structures of the Escherichia coli PPAT have been determined in the presence of either ATP or Ppant. Structural details of the catalytic center revealed specific roles for individual amino acid residues involved in substrate binding and catalysis. The side-chain of His18 stabilizes the expected pentacovalent intermediate, whereas the side-chains of Thr10 and Lys42 orient the nucleophile for an in-line displacement mechanism. The binding site for the manganese ion that interacts with the phosphate groups of the nucleotide has also been identified. Within the PPAT hexamer, one trimer is in its substrate-free state, whereas the other is in a substrate-bound state.
| | The line below this paragraph, {{ABSTRACT_PUBMED_11812124}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 11812124 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_11812124}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Nucleotidyltransferase]] | | [[Category: Nucleotidyltransferase]] |
| [[Category: Transferase]] | | [[Category: Transferase]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 17:46:29 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 05:32:50 2008'' |