1h17: Difference between revisions
New page: left|200px<br /> <applet load="1h17" size="450" color="white" frame="true" align="right" spinBox="true" caption="1h17, resolution 1.75Å" /> '''PYRUVATE FORMATE-LY... |
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caption="1h17, resolution 1.75Å" /> | caption="1h17, resolution 1.75Å" /> | ||
'''PYRUVATE FORMATE-LYASE (E.COLI) IN COMPLEX WITH COA AND THE SUBSTRATE ANALOG OXAMATE'''<br /> | '''PYRUVATE FORMATE-LYASE (E.COLI) IN COMPLEX WITH COA AND THE SUBSTRATE ANALOG OXAMATE'''<br /> | ||
==Overview== | |||
The glycyl radical enzyme pyruvate formate-lyase (PFL) synthesizes, acetyl-CoA and formate from pyruvate and CoA. With the crystal structure, of the non-radical form of PFL in complex with its two substrates, we have, trapped the moment prior to pyruvate cleavage. The structure reveals how, the active site aligns the scissile bond of pyruvate for radical attack, prevents non-radical side reactions of the pyruvate, and confines radical, migration. The structure shows CoA in a syn conformation awaiting pyruvate, cleavage. By changing to an anti conformation, without affecting the, adenine binding mode of CoA, the thiol of CoA could pick up the acetyl, group resulting from pyruvate cleavage. | |||
==About this Structure== | ==About this Structure== | ||
1H17 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 NA, MG, COA, OXM, DTL and PG4 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=2.3.1.54 2.3.1.54]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1H17 OCA]]. | 1H17 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 NA, MG, COA, OXM, DTL and PG4 as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/Formate_C-acetyltransferase Formate C-acetyltransferase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.54 2.3.1.54]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1H17 OCA]]. | ||
==Reference== | |||
X-ray structure of pyruvate formate-lyase in complex with pyruvate and CoA. How the enzyme uses the Cys-418 thiyl radical for pyruvate cleavage., Becker A, Kabsch W, J Biol Chem. 2002 Oct 18;277(42):40036-42. Epub 2002 Aug 5. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12163496 12163496] | |||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Formate C-acetyltransferase]] | |||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Becker, A.]] | [[Category: Becker, A.]] | ||
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[[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 11:07:56 2007'' | ||
Revision as of 12:03, 30 October 2007
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PYRUVATE FORMATE-LYASE (E.COLI) IN COMPLEX WITH COA AND THE SUBSTRATE ANALOG OXAMATE
OverviewOverview
The glycyl radical enzyme pyruvate formate-lyase (PFL) synthesizes, acetyl-CoA and formate from pyruvate and CoA. With the crystal structure, of the non-radical form of PFL in complex with its two substrates, we have, trapped the moment prior to pyruvate cleavage. The structure reveals how, the active site aligns the scissile bond of pyruvate for radical attack, prevents non-radical side reactions of the pyruvate, and confines radical, migration. The structure shows CoA in a syn conformation awaiting pyruvate, cleavage. By changing to an anti conformation, without affecting the, adenine binding mode of CoA, the thiol of CoA could pick up the acetyl, group resulting from pyruvate cleavage.
About this StructureAbout this Structure
1H17 is a [Single protein] structure of sequence from [Escherichia coli] with NA, MG, COA, OXM, DTL and PG4 as [ligands]. Active as [Formate C-acetyltransferase], with EC number [2.3.1.54]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
ReferenceReference
X-ray structure of pyruvate formate-lyase in complex with pyruvate and CoA. How the enzyme uses the Cys-418 thiyl radical for pyruvate cleavage., Becker A, Kabsch W, J Biol Chem. 2002 Oct 18;277(42):40036-42. Epub 2002 Aug 5. PMID:12163496
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