2g1h

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[[Image:2g1h.gif|left|200px]]
[[Image:2g1h.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 2g1h |SIZE=350|CAPTION= <scene name='initialview01'>2g1h</scene>, resolution 1.86&Aring;
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The line below this paragraph, containing "STRUCTURE_2g1h", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE= fabD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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-->
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|DOMAIN=
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{{STRUCTURE_2g1h| PDB=2g1h | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2g1h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2g1h OCA], [http://www.ebi.ac.uk/pdbsum/2g1h PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2g1h RCSB]</span>
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}}
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'''Structure of E.coli FabD complexed with glycerol'''
'''Structure of E.coli FabD complexed with glycerol'''
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: [Acyl-carrier-protein] S-malonyltransferase]]
 
[[Category: Oefner, C.]]
[[Category: Oefner, C.]]
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[[Category: complex]]
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[[Category: Complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 04:35:22 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:10:30 2008''
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Revision as of 01:35, 4 May 2008

Image:2g1h.gif

Template:STRUCTURE 2g1h

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 Page seeded by OCA on Sun May 4 04:35:22 2008

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