Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

1L2U

Orotidine 5'-monophosphate decarboxylase from E. coli

Summary for 1L2U
Entry DOI10.2210/pdb1l2u/pdb
Related1EIX 1JJK
DescriptorOrotidine 5'-phosphate decarboxylase (2 entities in total)
Functional Keywordsbeta-alpha-barrel, homodimer, twinned crystals, lyase
Biological sourceEscherichia coli
Total number of polymer chains2
Total formula weight52756.45
Authors
Harris, P.,Poulsen, J.C.,Jensen, K.F.,Larsen, S. (deposition date: 2002-02-25, release date: 2002-03-13, Last modification date: 2023-08-16)
Primary citationHarris, P.,Poulsen, J.C.,Jensen, K.F.,Larsen, S.
Substrate binding induces domain movements in orotidine 5'-monophosphate decarboxylase
J.Mol.Biol., 18:1019-1029, 2002
Cited by
PubMed Abstract: 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.
PubMed: 12054799
DOI: 10.1016/S0022-2836(02)00200-0
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.5 Å)
Structure validation

229564

PDB entries from 2025-01-01

PDB statisticsPDBj update infoContact PDBjnumon