1hnh

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[[Image:1hnh.jpg|left|200px]]
[[Image:1hnh.jpg|left|200px]]
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{{Structure
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|PDB= 1hnh |SIZE=350|CAPTION= <scene name='initialview01'>1hnh</scene>, resolution 1.9&Aring;
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The line below this paragraph, containing "STRUCTURE_1hnh", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SCY:S-ACETYL-CYSTEINE'>SCY</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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or leave the SCENE parameter empty for the default display.
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{{STRUCTURE_1hnh| PDB=1hnh | SCENE= }}
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|RELATEDENTRY=[[1hn9|1hn9]], [[1hnd|1hnd]], [[1hnj|1hnj]], [[1hnk|1hnk]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hnh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hnh OCA], [http://www.ebi.ac.uk/pdbsum/1hnh PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1hnh RCSB]</span>
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}}
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'''CRYSTAL STRUCTURE OF BETA-KETOACYL-ACP SYNTHASE III + DEGRADED FORM OF ACETYL-COA'''
'''CRYSTAL STRUCTURE OF BETA-KETOACYL-ACP SYNTHASE III + DEGRADED FORM OF ACETYL-COA'''
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[[Category: Qiu, X.]]
[[Category: Qiu, X.]]
[[Category: Smith, W W.]]
[[Category: Smith, W W.]]
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[[Category: fabh]]
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[[Category: Fabh]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:02:32 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:07:57 2008''
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Revision as of 16:02, 2 May 2008

Image:1hnh.jpg

Template:STRUCTURE 1hnh

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. 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 Fri May 2 19:02:32 2008

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