1h18
From Proteopedia
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|PDB= 1h18 |SIZE=350|CAPTION= <scene name='initialview01'>1h18</scene>, resolution 2.3Å | |PDB= 1h18 |SIZE=350|CAPTION= <scene name='initialview01'>1h18</scene>, resolution 2.3Å | ||
|SITE= <scene name='pdbsite=418:Pg4+Binding+Site+For+Chain+B'>418</scene> | |SITE= <scene name='pdbsite=418:Pg4+Binding+Site+For+Chain+B'>418</scene> | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=DTL:D-TREITOL'>DTL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=PYR:PYRUVIC+ACID'>PYR</scene> |
| - | |ACTIVITY= [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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1h18 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h18 OCA], [http://www.ebi.ac.uk/pdbsum/1h18 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1h18 RCSB]</span> | ||
}} | }} | ||
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[[Category: Becker, A.]] | [[Category: Becker, A.]] | ||
[[Category: Kabsch, W.]] | [[Category: Kabsch, W.]] | ||
| - | [[Category: DTL]] | ||
| - | [[Category: NA]] | ||
| - | [[Category: PG4]] | ||
| - | [[Category: PYR]] | ||
[[Category: acetylation]] | [[Category: acetylation]] | ||
[[Category: acyltransferase]] | [[Category: acyltransferase]] | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:55:40 2008'' |
Revision as of 17:55, 30 March 2008
| |||||||
| , resolution 2.3Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , , , | ||||||
| Activity: | Formate C-acetyltransferase, with EC number 2.3.1.54 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
PYRUVATE FORMATE-LYASE (E.COLI) IN COMPLEX WITH PYRUVATE
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
1H18 is a Single protein structure of sequence from Escherichia coli. 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
Page seeded by OCA on Sun Mar 30 20:55:40 2008
