1l2u

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[[Image:1l2u.jpg|left|200px]]
[[Image:1l2u.jpg|left|200px]]
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{{Structure
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|PDB= 1l2u |SIZE=350|CAPTION= <scene name='initialview01'>1l2u</scene>, resolution 2.5&Aring;
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The line below this paragraph, containing "STRUCTURE_1l2u", creates the "Structure Box" on the page.
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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_1l2u| PDB=1l2u | SCENE= }}
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|RELATEDENTRY=[[1eix|1EIX]], [[1jjk|1JJK]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1l2u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l2u OCA], [http://www.ebi.ac.uk/pdbsum/1l2u PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1l2u RCSB]</span>
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'''Orotidine 5'-monophosphate decarboxylase from E. coli'''
'''Orotidine 5'-monophosphate decarboxylase from E. coli'''
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[[Category: Larsen, S.]]
[[Category: Larsen, S.]]
[[Category: Poulsen, J C.]]
[[Category: Poulsen, J C.]]
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[[Category: beta-alpha-barrel]]
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[[Category: Beta-alpha-barrel]]
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[[Category: homodimer]]
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[[Category: Homodimer]]
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[[Category: twinned crystal]]
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[[Category: Twinned crystal]]
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[[Category: x-ray diffraction]]
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[[Category: X-ray diffraction]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 23:28:46 2008''
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Revision as of 20:28, 2 May 2008

Image:1l2u.jpg

Template:STRUCTURE 1l2u

Orotidine 5'-monophosphate decarboxylase from E. coli


Overview

Orotidine 5'-monophosphate decarboxylase (ODCase) catalyses the decarboxylation of orotidine 5'-monophosphate to uridine 5'-monophosphate (UMP). We have earlier determined the structure of ODCase from Escherichia coli complexed with the inhibitor 1-(5'-phospho-beta-d-ribofuranosyl)barbituric acid (BMP); here we present the 2.5 A structure of the uncomplexed apo enzyme, determined from twinned crystals. A structural analysis and comparison of the two structures of the E. coli enzyme show that binding of the inhibitor is accompanied by significant domain movements of approximately 12 degrees around a hinge that crosses the active site. Hence, the ODCase dimer, which contains two active sites, may be divided in three domains: a central domain that is fixed, and two lids which independently move 12 degrees upon binding. Corresponding analyses, presented herein, of the two Saccharomyces cerevisiae ODCase structures (with and without BMP) and the Methanobacterium thermoautotrophicum ODCase structures (with and without 6-aza UMP) show very similar, but somewhat smaller domain movements. The domain movements seem to be initiated by the phosphoryl binding to the enzyme and can explain why the binding of the phosphoryl group is essential for the catalytic function.

About this Structure

1L2U is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Substrate binding induces domain movements in orotidine 5'-monophosphate decarboxylase., Harris P, Poulsen JC, Jensen KF, Larsen S, J Mol Biol. 2002 May 10;318(4):1019-29. PMID:12054799 Page seeded by OCA on Fri May 2 23:28:46 2008

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