2g1h
From Proteopedia
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| - | [[Image:2g1h.gif|left|200px]] | + | [[Image:2g1h.gif|left|200px]] |
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| - | '''Structure of E.coli FabD complexed with glycerol''' | + | {{Structure |
| + | |PDB= 2g1h |SIZE=350|CAPTION= <scene name='initialview01'>2g1h</scene>, resolution 1.86Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/[Acyl-carrier-protein]_S-malonyltransferase [Acyl-carrier-protein] S-malonyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.39 2.3.1.39] | ||
| + | |GENE= fabD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | }} | ||
| + | |||
| + | '''Structure of E.coli FabD complexed with glycerol''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2G1H is a [ | + | 2G1H is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2G1H OCA]. |
==Reference== | ==Reference== | ||
| - | Mapping the active site of Escherichia coli malonyl-CoA-acyl carrier protein transacylase (FabD) by protein crystallography., Oefner C, Schulz H, D'Arcy A, Dale GE, Acta Crystallogr D Biol Crystallogr. 2006 Jun;62(Pt 6):613-8. Epub 2006, May 12. PMID:[http:// | + | Mapping the active site of Escherichia coli malonyl-CoA-acyl carrier protein transacylase (FabD) by protein crystallography., Oefner C, Schulz H, D'Arcy A, Dale GE, Acta Crystallogr D Biol Crystallogr. 2006 Jun;62(Pt 6):613-8. Epub 2006, May 12. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16699188 16699188] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: complex]] | [[Category: complex]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:59:17 2008'' |
Revision as of 14:59, 20 March 2008
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| , resolution 1.86Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | fabD (Escherichia coli) | ||||||
| Activity: | [Acyl-carrier-protein_S-malonyltransferase [Acyl-carrier-protein] S-malonyltransferase], with EC number 2.3.1.39 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Structure of E.coli FabD complexed with glycerol
Overview
Malonyl-CoA-acyl carrier protein transacylase (FabD; EC 2.3.1.39) is a key enzyme in the fatty-acid biosynthesis pathway of bacteria, catalyzing the transfer of a malonyl moiety from malonyl-CoA to holo acyl carrier protein (ACP), generating malonyl-ACP and free CoASH. Malonyl-ACP, which is the product of this reaction, is the key building block for de novo fatty-acid biosynthesis. Various binary complex structures of the Escherichia coli enzyme are presented, including that of the natural substrate malonyl-CoA, indicating the functional role of the highly conserved amino acids Gln11, Ser92, Arg117 and His201 and the stabilizing function of the preformed oxyanion hole during the enzymatic reaction. Based on the presented structural data, a possible new catalytic enzyme mechanism is discussed. The data obtained could be used in aiding the process of rational inhibitor design.
About this Structure
2G1H is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Mapping the active site of Escherichia coli malonyl-CoA-acyl carrier protein transacylase (FabD) by protein crystallography., Oefner C, Schulz H, D'Arcy A, Dale GE, Acta Crystallogr D Biol Crystallogr. 2006 Jun;62(Pt 6):613-8. Epub 2006, May 12. PMID:16699188[[Category: [Acyl-carrier-protein] S-malonyltransferase]]
Page seeded by OCA on Thu Mar 20 16:59:17 2008
