2g2z
From Proteopedia
(New page: 200px<br /><applet load="2g2z" size="450" color="white" frame="true" align="right" spinBox="true" caption="2g2z, resolution 2.80Å" /> '''Structure of E.coli ...) |
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| - | [[Image:2g2z.gif|left|200px]]<br /><applet load="2g2z" size=" | + | [[Image:2g2z.gif|left|200px]]<br /><applet load="2g2z" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2g2z, resolution 2.80Å" /> | caption="2g2z, resolution 2.80Å" /> | ||
'''Structure of E.coli FabD complexed with malonyl-CoA'''<br /> | '''Structure of E.coli FabD complexed with malonyl-CoA'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Malonyl-CoA-acyl carrier protein transacylase (FabD; EC 2.3.1.39) is a key | + | 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== | ==About this Structure== | ||
| - | 2G2Z 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 COZ and MLA as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http:// | + | 2G2Z 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 <scene name='pdbligand=COZ:'>COZ</scene> and <scene name='pdbligand=MLA:'>MLA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2G2Z OCA]. |
==Reference== | ==Reference== | ||
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[[Category: complex]] | [[Category: complex]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:27:37 2008'' |
Revision as of 15:27, 21 February 2008
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Structure of E.coli FabD complexed with malonyl-CoA
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
2G2Z is a Single protein structure of sequence from Escherichia coli with and as ligands. Active as [Acyl-carrier-protein_S-malonyltransferase [Acyl-carrier-protein] S-malonyltransferase], with EC number 2.3.1.39 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]]
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