1otf

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[[Image:1otf.jpg|left|200px]]
[[Image:1otf.jpg|left|200px]]
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{{Structure
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The line below this paragraph, containing "STRUCTURE_1otf", creates the "Structure Box" on the page.
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|GENE= DMPL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=306 Pseudomonas sp.])
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{{STRUCTURE_1otf| PDB=1otf | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1otf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1otf OCA], [http://www.ebi.ac.uk/pdbsum/1otf PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1otf RCSB]</span>
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'''4-OXALOCROTONATE TAUTOMERASE-TRICLINIC CRYSTAL FORM'''
'''4-OXALOCROTONATE TAUTOMERASE-TRICLINIC CRYSTAL FORM'''
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[[Category: Wigley, D B.]]
[[Category: Wigley, D B.]]
[[Category: Wilson, K S.]]
[[Category: Wilson, K S.]]
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[[Category: tautomerase]]
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[[Category: Tautomerase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 04:15:45 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:50:10 2008''
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Revision as of 01:15, 3 May 2008

Image:1otf.jpg

Template:STRUCTURE 1otf

4-OXALOCROTONATE TAUTOMERASE-TRICLINIC CRYSTAL FORM


Overview

5-Carboxymethyl-2-hydroxymuconate isomerase (CHMI) and 4-oxalocrotonate tautomerase (4-OT) are enzymes that catalyze the isomerization of unsaturated ketones. They share a common enzyme mechanism, although they show a preference for different substrates. There is no apparent sequence homology between the enzymes. To investigate the molecular mechanism and the basis for their substrate specificity, we have determined the crystal structures of the two enzymes at high resolution. 4-OT is hexameric, with the subunits arranged with 32 symmetry. CHMI is trimeric and has extensive contacts between subunits, which include secondary structural elements. The central core of the CHMI monomer has a fold similar to a 4-OT dimer, but the secondary structural elements that form the subunit contacts around the 3-fold axis are different in the two enzymes. The region of greatest similarity between the two enzymes is a large pocket that is proposed to be the active site. The enzymes appear to operate via a "one-base" mechanism, and the possible role of residues in this pocket is discussed in view of this idea. Finally, the molecular basis for substrate specificity in the two enzymes is discussed.

About this Structure

1OTF is a Single protein structure of sequence from Pseudomonas sp.. Full crystallographic information is available from OCA.

Reference

Enzymatic ketonization of 2-hydroxymuconate: specificity and mechanism investigated by the crystal structures of two isomerases., Subramanya HS, Roper DI, Dauter Z, Dodson EJ, Davies GJ, Wilson KS, Wigley DB, Biochemistry. 1996 Jan 23;35(3):792-802. PMID:8547259 Page seeded by OCA on Sat May 3 04:15:45 2008

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