1eix

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[[Image:1eix.jpg|left|200px]]
[[Image:1eix.jpg|left|200px]]
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{{Structure
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|PDB= 1eix |SIZE=350|CAPTION= <scene name='initialview01'>1eix</scene>, resolution 2.5&Aring;
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The line below this paragraph, containing "STRUCTURE_1eix", creates the "Structure Box" on the page.
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|SITE=
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|LIGAND= <scene name='pdbligand=BMQ:1-(5&#39;-PHOSPHO-BETA-D-RIBOFURANOSYL)BARBITURIC+ACID'>BMQ</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/Orotidine-5'-phosphate_decarboxylase Orotidine-5'-phosphate decarboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.23 4.1.1.23] </span>
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{{STRUCTURE_1eix| PDB=1eix | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1eix FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eix OCA], [http://www.ebi.ac.uk/pdbsum/1eix PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1eix RCSB]</span>
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'''STRUCTURE OF OROTIDINE 5'-MONOPHOSPHATE DECARBOXYLASE FROM E. COLI, CO-CRYSTALLISED WITH THE INHIBITOR BMP'''
'''STRUCTURE OF OROTIDINE 5'-MONOPHOSPHATE DECARBOXYLASE FROM E. COLI, CO-CRYSTALLISED WITH THE INHIBITOR BMP'''
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[[Category: Larsen, S.]]
[[Category: Larsen, S.]]
[[Category: Poulsen, J C.N.]]
[[Category: Poulsen, J C.N.]]
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[[Category: alpha-beta-barrel]]
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[[Category: Alpha-beta-barrel]]
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[[Category: homodimer]]
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[[Category: Homodimer]]
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[[Category: protein-inhibitor complex]]
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[[Category: Protein-inhibitor complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:09:14 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:03:28 2008''
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Revision as of 12:09, 2 May 2008

Image:1eix.jpg

Template:STRUCTURE 1eix

STRUCTURE OF OROTIDINE 5'-MONOPHOSPHATE DECARBOXYLASE FROM E. COLI, CO-CRYSTALLISED WITH THE INHIBITOR BMP


Overview

Orotidine 5'-monophosphate decarboxylase (ODCase) catalyzes the decarboxylation of orotidine 5'-monophosphate, the last step in the de novo synthesis of uridine 5'-monophosphate. ODCase is a very proficient enzyme [Radzicka, A., and Wolfenden, R. (1995) Science 267, 90-93], enhancing the reaction rate by a factor of 10(17). This proficiency has been enigmatic, since it is achieved without metal ions or cofactors. Here we present a 2.5 A resolution structure of ODCase complexed with the inhibitor 1-(5'-phospho-beta-D-ribofuranosyl)barbituric acid. It shows a closely packed dimer composed of two alpha/beta-barrels with two shared active sites. The orientation of the orotate moiety of the substrate is unambiguously deduced from the structure, and previously proposed catalytic mechanisms involving protonation of O2 or O4 can be ruled out. The proximity of the OMP carboxylate group with Asp71 appears to be instrumental for the decarboxylation of OMP, either through charge repulsion or through the formation of a very short O.H.O hydrogen bond between the two carboxylate groups.

About this Structure

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

Reference

Structural basis for the catalytic mechanism of a proficient enzyme: orotidine 5'-monophosphate decarboxylase., Harris P, Navarro Poulsen JC, Jensen KF, Larsen S, Biochemistry. 2000 Apr 18;39(15):4217-24. PMID:10757968 Page seeded by OCA on Fri May 2 15:09:14 2008

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