1hnk
From Proteopedia
(New page: 200px<br /> <applet load="1hnk" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hnk, resolution 1.9Å" /> '''CRYSTAL STRUCTURE OF...) |
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caption="1hnk, resolution 1.9Å" /> | caption="1hnk, resolution 1.9Å" /> | ||
'''CRYSTAL STRUCTURE OF BETA-KETOACYL-ACP SYNTHASE III, APO TETRAGONAL FORM'''<br /> | '''CRYSTAL STRUCTURE OF BETA-KETOACYL-ACP SYNTHASE III, APO TETRAGONAL FORM'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1HNK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. 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:// | + | 1HNK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. 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=1HNK OCA]. |
==Reference== | ==Reference== | ||
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[[Category: fabh]] | [[Category: fabh]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:57:21 2008'' |
Revision as of 13:57, 15 February 2008
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CRYSTAL STRUCTURE OF BETA-KETOACYL-ACP SYNTHASE III, APO TETRAGONAL FORM
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
1HNK is a Single protein structure of sequence from Escherichia coli. 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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