1gn8: Difference between revisions
New page: left|200px<br /> <applet load="1gn8" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gn8, resolution 1.83Å" /> '''PHOSPHOPANTETHEINE ... |
No edit summary |
||
| Line 8: | Line 8: | ||
==About this Structure== | ==About this Structure== | ||
1GN8 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]] with SO4, MN and ATP as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.3 2.7.7.3]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GN8 OCA]]. | 1GN8 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]] with SO4, MN and ATP as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[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]]. Structure known Active Site: ATA. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GN8 OCA]]. | ||
==Reference== | ==Reference== | ||
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11812124 11812124] | 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11812124 11812124] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Pantetheine-phosphate adenylyltransferase]] | |||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Izard, T.]] | [[Category: Izard, T.]] | ||
| Line 22: | Line 23: | ||
[[Category: transferase]] | [[Category: transferase]] | ||
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 13:23:21 2007'' | ||
Revision as of 14:18, 30 October 2007
|
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 ... [(full description)]
About this StructureAbout this Structure
1GN8 is a [Single protein] structure of sequence from [Escherichia coli] with SO4, MN and ATP as [ligands]. Active as [Pantetheine-phosphate adenylyltransferase], with EC number [2.7.7.3]. Structure known Active Site: ATA. 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
Page seeded by OCA on Tue Oct 30 13:23:21 2007