1gn8: Difference between revisions
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|PDB= 1gn8 |SIZE=350|CAPTION= <scene name='initialview01'>1gn8</scene>, resolution 1.83Å | |PDB= 1gn8 |SIZE=350|CAPTION= <scene name='initialview01'>1gn8</scene>, resolution 1.83Å | ||
|SITE= <scene name='pdbsite=ATA:Atp+Binding+Site+For+Chain+B'>ATA</scene> | |SITE= <scene name='pdbsite=ATA:Atp+Binding+Site+For+Chain+B'>ATA</scene> | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=ATP:ADENOSINE-5'-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> | ||
|ACTIVITY= [http://en.wikipedia.org/wiki/Pantetheine-phosphate_adenylyltransferase Pantetheine-phosphate adenylyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.3 2.7.7.3] | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Pantetheine-phosphate_adenylyltransferase Pantetheine-phosphate adenylyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.3 2.7.7.3] </span> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1gn8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gn8 OCA], [http://www.ebi.ac.uk/pdbsum/1gn8 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1gn8 RCSB]</span> | |||
}} | }} | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Izard, T.]] | [[Category: Izard, T.]] | ||
[[Category: coenzyme a biosynthesis]] | [[Category: coenzyme a biosynthesis]] | ||
[[Category: nucleotidyltransferase]] | [[Category: nucleotidyltransferase]] | ||
[[Category: transferase]] | [[Category: transferase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:47:34 2008'' | ||
Revision as of 20:47, 30 March 2008
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| , resolution 1.83Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , , | ||||||
| Activity: | Pantetheine-phosphate adenylyltransferase, with EC number 2.7.7.3 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
PHOSPHOPANTETHEINE ADENYLYLTRANSFERASE IN COMPLEX WITH MN2+ ATP FROM ESCHERICHIA COLI
OverviewOverview
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.
About this StructureAbout this Structure
1GN8 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
ReferenceReference
The crystal structures of phosphopantetheine adenylyltransferase with bound substrates reveal the enzyme's catalytic mechanism., Izard T, J Mol Biol. 2002 Jan 25;315(4):487-95. PMID:11812124
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