1hnd
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:1hnd.jpg|left|200px]] | + | [[Image:1hnd.jpg|left|200px]] |
| - | + | ||
| - | '''CRYSTAL STRUCTURE OF BETA-KETOACYL-ACP SYNTHASE III-COA COMPLEX''' | + | {{Structure |
| + | |PDB= 1hnd |SIZE=350|CAPTION= <scene name='initialview01'>1hnd</scene>, resolution 1.6Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=COA:COENZYME A'>COA</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-COA COMPLEX''' | ||
| + | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1HND is a [ | + | 1HND is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HND OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11243824 11243824] |
[[Category: Beta-ketoacyl-acyl-carrier-protein synthase I]] | [[Category: Beta-ketoacyl-acyl-carrier-protein synthase I]] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
| Line 23: | Line 32: | ||
[[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 11:39:19 2008'' |
Revision as of 09:39, 20 March 2008
| |||||||
| , resolution 1.6Å | |||||||
|---|---|---|---|---|---|---|---|
| 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-COA COMPLEX
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
1HND is a Single protein structure of sequence from Escherichia coli. 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
Page seeded by OCA on Thu Mar 20 11:39:19 2008
