1gyy
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:1gyy.gif|left|200px]]<br /><applet load="1gyy" size=" | + | [[Image:1gyy.gif|left|200px]]<br /><applet load="1gyy" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1gyy, resolution 1.35Å" /> | caption="1gyy, resolution 1.35Å" /> | ||
'''THE CRYSTAL STRUCTURE OF YDCE, A 4-OXALOCROTONATE TAUTOMERASE HOMOLOGUE FROM ESCHERICHIA COLI, CONFIRMS THE STRUCTURAL BASIS FOR OLIGOMER DIVERSITY'''<br /> | '''THE CRYSTAL STRUCTURE OF YDCE, A 4-OXALOCROTONATE TAUTOMERASE HOMOLOGUE FROM ESCHERICHIA COLI, CONFIRMS THE STRUCTURAL BASIS FOR OLIGOMER DIVERSITY'''<br /> | ||
| Line 7: | Line 7: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1GYY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with FHC as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Phenylpyruvate_tautomerase Phenylpyruvate tautomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.2.1 5.3.2.1] Known structural/functional Site: <scene name='pdbsite=FHA:Fhc Binding Site For Chain B'>FHA</scene>. Full crystallographic information is available from [http:// | + | 1GYY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=FHC:'>FHC</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Phenylpyruvate_tautomerase Phenylpyruvate tautomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.2.1 5.3.2.1] Known structural/functional Site: <scene name='pdbsite=FHA:Fhc+Binding+Site+For+Chain+B'>FHA</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GYY OCA]. |
==Reference== | ==Reference== | ||
| Line 28: | Line 28: | ||
[[Category: tautomerase]] | [[Category: tautomerase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:44:09 2008'' |
Revision as of 07:44, 3 February 2008
|
THE CRYSTAL STRUCTURE OF YDCE, A 4-OXALOCROTONATE TAUTOMERASE HOMOLOGUE FROM ESCHERICHIA COLI, CONFIRMS THE STRUCTURAL BASIS FOR OLIGOMER DIVERSITY
Overview
The tautomerase superfamily consists of three major families represented, by 4-oxalocrotonate tautomerase (4-OT), 5-(carboxymethyl)-2-hydroxymuconate isomerase (CHMI), and macrophage, migration inhibitory factor (MIF). The members of this superfamily are, structurally homologous proteins constructed from a simple beta-alpha-beta, fold that share a key mechanistic feature; they use an amino-terminal, proline, which has an unusually low pK(a), as the general base in a, keto-enol tautomerization. Several new members of the 4-OT family have now, been identified using PSI-BLAST and categorized into five subfamilies on, the basis of multiple-sequence alignments and the conservation of key, catalytic and structural residues. The members of subfamily 5, which, includes a hypothetical protein designated YdcE from Escherichia coli, are, predicted not to form hexamers. The crystal structure of YdcE has been, determined to 1.35 A resolution and confirms that it is a dimer. In, addition, YdcE complexed with (E)-2-fluoro-p-hydroxycinnamate, identified, as a potent competitive inhibitor of this enzyme, as well as, N-(2-hydroxyethyl)piperazine-N'-2-ethanesulfonic acid (HEPES) and benzoate, are also presented. These latter crystal structures reveal the location of, the active site and suggest a mechanism for the observed YdcE-catalyzed, tautomerization reaction. The dimeric arrangement of YdcE represents a new, structure in the 4-OT family and demonstrates structural diversity within, the 4-OT family not previously reported.
About this Structure
1GYY is a Single protein structure of sequence from Escherichia coli with as ligand. Active as Phenylpyruvate tautomerase, with EC number 5.3.2.1 Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
The crystal structure of YdcE, a 4-oxalocrotonate tautomerase homologue from Escherichia coli, confirms the structural basis for oligomer diversity., Almrud JJ, Kern AD, Wang SC, Czerwinski RM, Johnson WH Jr, Murzin AG, Hackert ML, Whitman CP, Biochemistry. 2002 Oct 8;41(40):12010-24. PMID:12356301
Page seeded by OCA on Sun Feb 3 09:44:09 2008
