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1xge

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[[Image:1xge.gif|left|200px]]<br /><applet load="1xge" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1xge.gif|left|200px]]
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caption="1xge, resolution 1.90&Aring;" />
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'''Dihydroorotase from Escherichia coli: Loop Movement and Cooperativity between subunits'''<br />
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{{Structure
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|PDB= 1xge |SIZE=350|CAPTION= <scene name='initialview01'>1xge</scene>, resolution 1.90&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=DOR:(4S)-2,6-DIOXOHEXAHYDROPYRIMIDINE-4-CARBOXYLIC+ACID'>DOR</scene> and <scene name='pdbligand=NCD:N-CARBAMOYL-L-ASPARTATE'>NCD</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Dihydroorotase Dihydroorotase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.2.3 3.5.2.3]
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|GENE= pyrC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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}}
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'''Dihydroorotase from Escherichia coli: Loop Movement and Cooperativity between subunits'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1XGE 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=ZN:'>ZN</scene>, <scene name='pdbligand=DOR:'>DOR</scene> and <scene name='pdbligand=NCD:'>NCD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Dihydroorotase Dihydroorotase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.2.3 3.5.2.3] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XGE OCA].
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1XGE is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XGE OCA].
==Reference==
==Reference==
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Dihydroorotase from Escherichia coli: loop movement and cooperativity between subunits., Lee M, Chan CW, Mitchell Guss J, Christopherson RI, Maher MJ, J Mol Biol. 2005 May 6;348(3):523-33. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15826651 15826651]
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Dihydroorotase from Escherichia coli: loop movement and cooperativity between subunits., Lee M, Chan CW, Mitchell Guss J, Christopherson RI, Maher MJ, J Mol Biol. 2005 May 6;348(3):523-33. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15826651 15826651]
[[Category: Dihydroorotase]]
[[Category: Dihydroorotase]]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: tim barrel]]
[[Category: tim barrel]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:54:33 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:09:27 2008''

Revision as of 13:09, 20 March 2008

Image:1xge.gif


PDB ID 1xge

Drag the structure with the mouse to rotate
, resolution 1.90Å
Ligands: , and
Gene: pyrC (Escherichia coli)
Activity: Dihydroorotase, with EC number 3.5.2.3
Coordinates: save as pdb, mmCIF, xml



Dihydroorotase from Escherichia coli: Loop Movement and Cooperativity between subunits


Overview

Escherichia coli dihydroorotase has been crystallized in the presence of the product, L-dihydroorotate (L-DHO), and the structure refined at 1.9A resolution. The structure confirms that previously reported (PDB entry 1J79), crystallized in the presence of the substrate N-carbamyl-D,L-aspartate (D, L-CA-asp), which had a dimer in the asymmetric unit, with one subunit having the substrate, L-CA-asp bound at the active site and the other having L-DHO. Importantly, no explanation for the unusual structure was given. Our results now show that a loop comprised of residues 105-115 has different conformations in the two subunits. In the case of the L-CA-asp-bound subunit, this loop reaches in toward the active site and makes hydrogen-bonding contact with the bound substrate molecule. For the L-DHO-bound subunit, the loop faces in the opposite direction and forms part of the surface of the protein. Analysis of the kinetics for conversion of L-DHO to L-CA-asp at low concentrations of L-DHO shows positive cooperativity with a Hill coefficient n=1.57(+/-0.13). Communication between subunits in the dimer may occur via cooperative conformational changes of the side-chains of a tripeptide from each subunit: Arg256-His257-Arg258, near the subunit interface.

About this Structure

1XGE is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Dihydroorotase from Escherichia coli: loop movement and cooperativity between subunits., Lee M, Chan CW, Mitchell Guss J, Christopherson RI, Maher MJ, J Mol Biol. 2005 May 6;348(3):523-33. PMID:15826651

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