1hn9
From Proteopedia
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| - | [[Image:1hn9.jpg|left|200px]] | + | [[Image:1hn9.jpg|left|200px]] |
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| - | '''CRYSTAL STRUCTURE OF BETA-KETOACYL-ACP SYNTHASE III''' | + | {{Structure |
| + | |PDB= 1hn9 |SIZE=350|CAPTION= <scene name='initialview01'>1hn9</scene>, resolution 2.Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=PO4:PHOSPHATE ION'>PO4</scene> | ||
| + | |ACTIVITY= [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] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''CRYSTAL STRUCTURE OF BETA-KETOACYL-ACP SYNTHASE III''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1HN9 is a [ | + | 1HN9 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. This structure supersedes the now removed PDB entry 1D9B. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HN9 OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10593943 10593943] |
[[Category: Beta-ketoacyl-acyl-carrier-protein synthase I]] | [[Category: Beta-ketoacyl-acyl-carrier-protein synthase I]] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
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[[Category: fabh]] | [[Category: fabh]] | ||
| - | ''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 11:39:13 2008'' |
Revision as of 09:39, 20 March 2008
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| , resolution 2.Å | |||||||
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| Ligands: | |||||||
| Activity: | Beta-ketoacyl-acyl-carrier-protein synthase I, with EC number 2.3.1.41 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. This structure supersedes the now removed PDB entry 1D9B. 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
Page seeded by OCA on Thu Mar 20 11:39:13 2008
