1pn2

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[[Image:1pn2.jpg|left|200px]]<br /><applet load="1pn2" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1pn2.jpg|left|200px]]
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caption="1pn2, resolution 1.95&Aring;" />
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'''Crystal structure analysis of the selenomethionine labelled 2-enoyl-CoA hydratase 2 domain of Candida tropicalis multifunctional enzyme type 2'''<br />
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{{Structure
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|PDB= 1pn2 |SIZE=350|CAPTION= <scene name='initialview01'>1pn2</scene>, resolution 1.95&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>
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|ACTIVITY=
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|GENE= FOX2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5482 Candida tropicalis])
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}}
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'''Crystal structure analysis of the selenomethionine labelled 2-enoyl-CoA hydratase 2 domain of Candida tropicalis multifunctional enzyme type 2'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1PN2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Candida_tropicalis Candida tropicalis] with <scene name='pdbligand=EDO:'>EDO</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PN2 OCA].
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1PN2 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Candida_tropicalis Candida tropicalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PN2 OCA].
==Reference==
==Reference==
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A two-domain structure of one subunit explains unique features of eukaryotic hydratase 2., Koski MK, Haapalainen AM, Hiltunen JK, Glumoff T, J Biol Chem. 2004 Jun 4;279(23):24666-72. Epub 2004 Mar 29. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15051722 15051722]
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A two-domain structure of one subunit explains unique features of eukaryotic hydratase 2., Koski MK, Haapalainen AM, Hiltunen JK, Glumoff T, J Biol Chem. 2004 Jun 4;279(23):24666-72. Epub 2004 Mar 29. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15051722 15051722]
[[Category: Candida tropicalis]]
[[Category: Candida tropicalis]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: hydratase 2 motif]]
[[Category: hydratase 2 motif]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:30:25 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:26:23 2008''

Revision as of 11:26, 20 March 2008


PDB ID 1pn2

Drag the structure with the mouse to rotate
, resolution 1.95Å
Ligands:
Gene: FOX2 (Candida tropicalis)
Coordinates: save as pdb, mmCIF, xml



Crystal structure analysis of the selenomethionine labelled 2-enoyl-CoA hydratase 2 domain of Candida tropicalis multifunctional enzyme type 2


Overview

2-Enoyl-CoA hydratase 2, a part from multifunctional enzyme type 2, hydrates trans-2-enoyl-CoA to 3-hydroxyacyl-CoA in the (3R)-hydroxy-dependent route of peroxisomal beta-oxidation of fatty acids. Unliganded and (3R)-hydroxydecanoyl coenzyme A-complexed crystal structures of 2-enoyl-CoA hydratase 2 from Candida tropicalis multifunctional enzyme type 2 were solved to 1.95- and 2.35-A resolution, respectively. 2-Enoyl-CoA hydratase 2 is a dimeric, alpha+beta protein with a novel quaternary structure. The overall structure of the two-domain subunit of eukaryotic 2-enoyl-CoA hydratase 2 resembles the homodimeric, hot dog fold structures of prokaryotic (R)-specific 2-enoyl-CoA hydratase and beta-hydroxydecanoyl thiol ester dehydrase. Importantly, though, the eukaryotic hydratase 2 has a complete hot dog fold only in its C-domain, whereas the N-domain lacks a long central alpha-helix, thus creating space for bulkier substrates in the binding pocket and explaining the observed difference in substrate preference between eukaryotic and prokaryotic enzymes. Although the N- and C-domains have an identity of <10% at the amino acid level, they share a 50% identity at the nucleotide level and fold similarly. We suggest that a subunit of 2-enoyl-CoA hydratase 2 has evolved via a gene duplication with the concomitant loss of one catalytic site. The hydrogen bonding network of the active site of 2-enoyl-CoA hydratase 2 resembles the active site geometry of mitochondrial (S)-specific 2-enoyl-CoA hydratase 1, although in a mirror image fashion. This arrangement allows the reaction to occur by similar mechanism, supported by mutagenesis and mechanistic studies, although via reciprocal stereochemistry.

About this Structure

1PN2 is a Single protein structure of sequence from Candida tropicalis. Full crystallographic information is available from OCA.

Reference

A two-domain structure of one subunit explains unique features of eukaryotic hydratase 2., Koski MK, Haapalainen AM, Hiltunen JK, Glumoff T, J Biol Chem. 2004 Jun 4;279(23):24666-72. Epub 2004 Mar 29. PMID:15051722

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