1u1z
From Proteopedia
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| - | [[Image:1u1z.jpg|left|200px]] | + | [[Image:1u1z.jpg|left|200px]] |
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| - | '''The Structure of (3R)-hydroxyacyl-ACP dehydratase (FabZ)''' | + | {{Structure |
| + | |PDB= 1u1z |SIZE=350|CAPTION= <scene name='initialview01'>1u1z</scene>, resolution 2.50Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= fabZ ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=287 Pseudomonas aeruginosa]) | ||
| + | }} | ||
| + | |||
| + | '''The Structure of (3R)-hydroxyacyl-ACP dehydratase (FabZ)''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1U1Z is a [ | + | 1U1Z is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. The following page contains interesting information on the relation of 1U1Z with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb90_1.html Fatty Acid Synthase]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U1Z OCA]. |
==Reference== | ==Reference== | ||
| - | The structure of (3R)-hydroxyacyl-acyl carrier protein dehydratase (FabZ) from Pseudomonas aeruginosa., Kimber MS, Martin F, Lu Y, Houston S, Vedadi M, Dharamsi A, Fiebig KM, Schmid M, Rock CO, J Biol Chem. 2004 Dec 10;279(50):52593-602. Epub 2004 Sep 14. PMID:[http:// | + | The structure of (3R)-hydroxyacyl-acyl carrier protein dehydratase (FabZ) from Pseudomonas aeruginosa., Kimber MS, Martin F, Lu Y, Houston S, Vedadi M, Dharamsi A, Fiebig KM, Schmid M, Rock CO, J Biol Chem. 2004 Dec 10;279(50):52593-602. Epub 2004 Sep 14. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15371447 15371447] |
[[Category: Fatty Acid Synthase]] | [[Category: Fatty Acid Synthase]] | ||
[[Category: Pseudomonas aeruginosa]] | [[Category: Pseudomonas aeruginosa]] | ||
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[[Category: dehydratase; fatty acid biosynthesis; hot dog fold]] | [[Category: dehydratase; fatty acid biosynthesis; hot dog fold]] | ||
| - | ''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 14:26:18 2008'' |
Revision as of 12:26, 20 March 2008
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| , resolution 2.50Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | fabZ (Pseudomonas aeruginosa) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
The Structure of (3R)-hydroxyacyl-ACP dehydratase (FabZ)
Overview
Type II fatty acid biosynthesis systems are essential for membrane formation in bacteria, making the constituent proteins of this pathway attractive targets for antibacterial drug discovery. The third step in the elongation cycle of the type II fatty acid biosynthesis is catalyzed by beta-hydroxyacyl-(acyl carrier protein) (ACP) dehydratase. There are two isoforms. FabZ, which catalyzes the dehydration of (3R)-hydroxyacyl-ACP to trans-2-acyl-ACP, is a universally expressed component of the bacterial type II system. FabA, the second isoform, as has more limited distribution in nature and, in addition to dehydration, also carries out the isomerization of trans-2- to cis-3-decenoyl-ACP as an essential step in unsaturated fatty acid biosynthesis. We report the structure of FabZ from the important human pathogen Pseudomonas aeruginosa at 2.5 A of resolution. PaFabZ is a hexamer (trimer of dimers) with the His/Glu catalytic dyad located within a deep, narrow tunnel formed at the dimer interface. Site-directed mutagenesis experiments showed that the obvious differences in the active site residues that distinguish the FabA and FabZ subfamilies of dehydratases do not account for the unique ability of FabA to catalyze isomerization. Because the catalytic machinery of the two enzymes is practically indistinguishable, the structural differences observed in the shape of the substrate binding channels of FabA and FabZ lead us to hypothesize that the different shapes of the tunnels control the conformation and positioning of the bound substrate, allowing FabA, but not FabZ, to catalyze the isomerization reaction.
About this Structure
1U1Z is a Single protein structure of sequence from Pseudomonas aeruginosa. The following page contains interesting information on the relation of 1U1Z with [Fatty Acid Synthase]. Full crystallographic information is available from OCA.
Reference
The structure of (3R)-hydroxyacyl-acyl carrier protein dehydratase (FabZ) from Pseudomonas aeruginosa., Kimber MS, Martin F, Lu Y, Houston S, Vedadi M, Dharamsi A, Fiebig KM, Schmid M, Rock CO, J Biol Chem. 2004 Dec 10;279(50):52593-602. Epub 2004 Sep 14. PMID:15371447
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