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==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.

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==

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[[Category: transferase]]

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@@ Line 4: / Line 4: @@
 ==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.
+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==
@@ Line 26: / Line 26: @@
 [[Category: transferase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb  3 09:45:03 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:56:14 2008''