1h17

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[[Image:1h17.gif|left|200px]]<br />
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[[Image:1h17.gif|left|200px]]<br /><applet load="1h17" size="450" color="white" frame="true" align="right" spinBox="true"
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<applet load="1h17" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1h17, resolution 1.75&Aring;" />
caption="1h17, resolution 1.75&Aring;" />
'''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 />
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==About this Structure==
==About this Structure==
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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].
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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] Known structural/functional Site: <scene name='pdbsite=AC1:Pg4 Binding Site For Chain A'>AC1</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1H17 OCA].
==Reference==
==Reference==
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[[Category: transferase]]
[[Category: transferase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 16:25:25 2007''
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 15:51:33 2007''

Revision as of 13:41, 18 December 2007


1h17, resolution 1.75Å

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PYRUVATE FORMATE-LYASE (E.COLI) IN COMPLEX WITH COA AND THE SUBSTRATE ANALOG OXAMATE

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

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 Known structural/functional Site: . Full crystallographic information is available from 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:12163496

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