1hn9
From Proteopedia
(New page: 200px<br /><applet load="1hn9" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hn9, resolution 2.Å" /> '''CRYSTAL STRUCTURE OF B...) |
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| - | [[Image:1hn9.jpg|left|200px]]<br /><applet load="1hn9" size=" | + | [[Image:1hn9.jpg|left|200px]]<br /><applet load="1hn9" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1hn9, resolution 2.Å" /> | caption="1hn9, resolution 2.Å" /> | ||
'''CRYSTAL STRUCTURE OF BETA-KETOACYL-ACP SYNTHASE III'''<br /> | '''CRYSTAL STRUCTURE OF BETA-KETOACYL-ACP SYNTHASE III'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Beta-ketoacyl-acyl carrier protein synthase III (FabH), the most divergent | + | Beta-ketoacyl-acyl carrier protein synthase III (FabH), the most divergent member of the family of condensing enzymes, is a key catalyst in bacterial fatty acid biosynthesis and a promising target for novel antibiotics. We report here the crystal structures of FabH determined in the presence and absence of acetyl-CoA. These structures display a fold that is common for condensing enzymes. The observed acetylation of Cys(112) proves its catalytic role and clearly defines the primer binding pocket. Modeling based on a bound CoA molecule suggests catalytic roles for His(244) and Asn(274). The structures provide the molecular basis for FabH substrate specificity and reaction mechanism and are important for structure-based design of novel antibiotics. |
==About this Structure== | ==About this Structure== | ||
| - | 1HN9 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 PO4 as [http://en.wikipedia.org/wiki/ligand ligand]. This structure | + | 1HN9 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=PO4:'>PO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. This structure supersedes the now removed PDB entry 1D9B. Active as [http://en.wikipedia.org/wiki/Beta-ketoacyl-acyl-carrier-protein_synthase_I Beta-ketoacyl-acyl-carrier-protein synthase I], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.41 2.3.1.41] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HN9 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Abdel-Meguid, S | + | [[Category: Abdel-Meguid, S S.]] |
| - | [[Category: Janson, C | + | [[Category: Janson, C A.]] |
| - | [[Category: Khandekar, S | + | [[Category: Khandekar, S K.]] |
| - | [[Category: Konstantinidis, A | + | [[Category: Konstantinidis, A K.]] |
[[Category: Lonsdale, J.]] | [[Category: Lonsdale, J.]] | ||
[[Category: Nwagwu, S.]] | [[Category: Nwagwu, S.]] | ||
[[Category: Qiu, X.]] | [[Category: Qiu, X.]] | ||
[[Category: Silverman, C.]] | [[Category: Silverman, C.]] | ||
| - | [[Category: Smith, W | + | [[Category: Smith, W W.]] |
[[Category: PO4]] | [[Category: PO4]] | ||
[[Category: fabh]] | [[Category: fabh]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:02:56 2008'' |
Revision as of 11:02, 21 February 2008
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CRYSTAL STRUCTURE OF BETA-KETOACYL-ACP SYNTHASE III
Overview
Beta-ketoacyl-acyl carrier protein synthase III (FabH), the most divergent member of the family of condensing enzymes, is a key catalyst in bacterial fatty acid biosynthesis and a promising target for novel antibiotics. We report here the crystal structures of FabH determined in the presence and absence of acetyl-CoA. These structures display a fold that is common for condensing enzymes. The observed acetylation of Cys(112) proves its catalytic role and clearly defines the primer binding pocket. Modeling based on a bound CoA molecule suggests catalytic roles for His(244) and Asn(274). The structures provide the molecular basis for FabH substrate specificity and reaction mechanism and are important for structure-based design of novel antibiotics.
About this Structure
1HN9 is a Single protein structure of sequence from Escherichia coli with as ligand. This structure supersedes the now removed PDB entry 1D9B. Active as Beta-ketoacyl-acyl-carrier-protein synthase I, with EC number 2.3.1.41 Full crystallographic information is available from OCA.
Reference
Crystal structure of beta-ketoacyl-acyl carrier protein synthase III. A key condensing enzyme in bacterial fatty acid biosynthesis., Qiu X, Janson CA, Konstantinidis AK, Nwagwu S, Silverman C, Smith WW, Khandekar S, Lonsdale J, Abdel-Meguid SS, J Biol Chem. 1999 Dec 17;274(51):36465-71. PMID:10593943
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