1hnh
From Proteopedia
(New page: 200px<br /><applet load="1hnh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hnh, resolution 1.9Å" /> '''CRYSTAL STRUCTURE OF ...) |
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| - | [[Image:1hnh.jpg|left|200px]]<br /><applet load="1hnh" size=" | + | [[Image:1hnh.jpg|left|200px]]<br /><applet load="1hnh" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1hnh, resolution 1.9Å" /> | caption="1hnh, resolution 1.9Å" /> | ||
'''CRYSTAL STRUCTURE OF BETA-KETOACYL-ACP SYNTHASE III + DEGRADED FORM OF ACETYL-COA'''<br /> | '''CRYSTAL STRUCTURE OF BETA-KETOACYL-ACP SYNTHASE III + DEGRADED FORM OF ACETYL-COA'''<br /> | ||
==Overview== | ==Overview== | ||
| - | beta-Ketoacyl-acyl carrier protein synthase III (FabH) is a condensing | + | beta-Ketoacyl-acyl carrier protein synthase III (FabH) is a condensing enzyme that plays central roles in fatty acid biosynthesis. Three-dimensional structures of E. coli FabH in the presence and absence of ligands have been refined to 1.46 A resolution. The structures of improved accuracy revealed detailed interactions involved in ligand binding. These structures also provided new insights into the FabH mechanism, e.g. the possible role of a water or hydroxyl anion in Cys112 deprotonation. A structure of the apo enzyme uncovered large conformational changes in the active site, exemplified by the disordering of four essential loops (84-86, 146-152, 185-217 and 305-307) and the movement of catalytic residues (Cys112 and His244). The disordering of the loops leads to greater than 50 % reduction in the FabH dimer interface, suggesting a dynamic nature for an unusually large portion of the dimer interface. The existence of a large solvent-accessible channel in the dimer interface as well as two cis-peptides (cis-Pro88 and cis-Phe308) in two of the disordered loops may explain the observed structural instabilities. |
==About this Structure== | ==About this Structure== | ||
| - | 1HNH 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 COA as [http://en.wikipedia.org/wiki/ligand ligand]. 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:// | + | 1HNH 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=COA:'>COA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. 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=1HNH OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Head, M.]] | [[Category: Head, M.]] | ||
| - | [[Category: Janson, C | + | [[Category: Janson, C A.]] |
| - | [[Category: Konstantinidis, A | + | [[Category: Konstantinidis, A K.]] |
[[Category: Lonsdale, J.]] | [[Category: Lonsdale, J.]] | ||
[[Category: Qiu, X.]] | [[Category: Qiu, X.]] | ||
| - | [[Category: Smith, W | + | [[Category: Smith, W W.]] |
[[Category: COA]] | [[Category: COA]] | ||
[[Category: fabh]] | [[Category: fabh]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:03:04 2008'' |
Revision as of 11:03, 21 February 2008
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CRYSTAL STRUCTURE OF BETA-KETOACYL-ACP SYNTHASE III + DEGRADED FORM OF ACETYL-COA
Overview
beta-Ketoacyl-acyl carrier protein synthase III (FabH) is a condensing enzyme that plays central roles in fatty acid biosynthesis. Three-dimensional structures of E. coli FabH in the presence and absence of ligands have been refined to 1.46 A resolution. The structures of improved accuracy revealed detailed interactions involved in ligand binding. These structures also provided new insights into the FabH mechanism, e.g. the possible role of a water or hydroxyl anion in Cys112 deprotonation. A structure of the apo enzyme uncovered large conformational changes in the active site, exemplified by the disordering of four essential loops (84-86, 146-152, 185-217 and 305-307) and the movement of catalytic residues (Cys112 and His244). The disordering of the loops leads to greater than 50 % reduction in the FabH dimer interface, suggesting a dynamic nature for an unusually large portion of the dimer interface. The existence of a large solvent-accessible channel in the dimer interface as well as two cis-peptides (cis-Pro88 and cis-Phe308) in two of the disordered loops may explain the observed structural instabilities.
About this Structure
1HNH is a Single protein structure of sequence from Escherichia coli with as ligand. Active as Beta-ketoacyl-acyl-carrier-protein synthase I, with EC number 2.3.1.41 Full crystallographic information is available from OCA.
Reference
Refined structures of beta-ketoacyl-acyl carrier protein synthase III., Qiu X, Janson CA, Smith WW, Head M, Lonsdale J, Konstantinidis AK, J Mol Biol. 2001 Mar 16;307(1):341-56. PMID:11243824
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