1hno

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[[Image:1hno.jpg|left|200px]]
[[Image:1hno.jpg|left|200px]]
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{{Structure
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|PDB= 1hno |SIZE=350|CAPTION= <scene name='initialview01'>1hno</scene>, resolution 2.5&Aring;
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The line below this paragraph, containing "STRUCTURE_1hno", 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=EDO:1,2-ETHANEDIOL'>EDO</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/Dodecenoyl-CoA_isomerase Dodecenoyl-CoA isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.3.8 5.3.3.8] </span>
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{{STRUCTURE_1hno| PDB=1hno | SCENE= }}
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|RELATEDENTRY=[[1hnu|1HNU]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hno FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hno OCA], [http://www.ebi.ac.uk/pdbsum/1hno PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1hno RCSB]</span>
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'''CRYSTAL STRUCTURE OF PEROXISOMAL DELTA3-DELTA2-ENOYL-COA ISOMERASE FROM SACCHAROMYCES CEREVISIAE'''
'''CRYSTAL STRUCTURE OF PEROXISOMAL DELTA3-DELTA2-ENOYL-COA ISOMERASE FROM SACCHAROMYCES CEREVISIAE'''
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[[Category: Mursula, A M.]]
[[Category: Mursula, A M.]]
[[Category: Wierenga, R K.]]
[[Category: Wierenga, R K.]]
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[[Category: alpha/beta]]
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[[Category: Alpha/beta]]
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[[Category: unliganded]]
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[[Category: Unliganded]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:02:49 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:08:03 2008''
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Revision as of 16:02, 2 May 2008

Image:1hno.jpg

Template:STRUCTURE 1hno

CRYSTAL STRUCTURE OF PEROXISOMAL DELTA3-DELTA2-ENOYL-COA ISOMERASE FROM SACCHAROMYCES CEREVISIAE


Overview

The active-site geometry of the first crystal structure of a Delta(3)-Delta(2)-enoyl-coenzyme A (CoA) isomerase (the peroxisomal enzyme from the yeast Saccharomyces cerevisiae) shows that only one catalytic base, Glu158, is involved in shuttling the proton from the C2 carbon atom of the substrate, Delta(3)-enoyl-CoA, to the C4 atom of the product, Delta(2)-enoyl-CoA. Site-directed mutagenesis has been performed to confirm that this glutamate residue is essential for catalysis. This Delta(3)-Delta(2)-enoyl-CoA isomerase is a hexameric enzyme, consisting of six identical subunits. It belongs to the hydratase/isomerase superfamily of enzymes which catalyze a wide range of CoA-dependent reactions. The members of the hydratase/ isomerase superfamily have only a low level of sequence identity. Comparison of the crystal structure of the Delta(3)-Delta(2)-enoyl-CoA isomerase with the other structures of this superfamily shows only one region of large structural variability, which is in the second turn of the spiral fold and which is involved in defining the shape of the binding pocket.

About this Structure

1HNO is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

The crystal structure of delta(3)-delta(2)-enoyl-CoA isomerase., Mursula AM, van Aalten DM, Hiltunen JK, Wierenga RK, J Mol Biol. 2001 Jun 15;309(4):845-53. PMID:11399063 Page seeded by OCA on Fri May 2 19:02:49 2008

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