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[[Image:1oro.jpg|left|200px]]<br /><applet load="1oro" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1oro, resolution 2.40&Aring;" />
'''A FLEXIBLE LOOP AT THE DIMER INTERFACE IS A PART OF THE ACTIVE SITE OF THE ADJACENT MONOMER OF ESCHERICHIA COLI OROTATE PHOSPHORIBOSYLTRANSFERASE'''<br />


==Overview==
==A FLEXIBLE LOOP AT THE DIMER INTERFACE IS A PART OF THE ACTIVE SITE OF THE ADJACENT MONOMER OF ESCHERICHIA COLI OROTATE PHOSPHORIBOSYLTRANSFERASE==
Orotate phosphoribosyltransferase (OPRTase) is involved in the biosynthesis of pyrimidine nucleotides. Alpha-D-ribosyldiphosphate 5-phosphate (PRPP) and orotate are utilized to form pyrophosphate and orotidine 5'-monophosphate (OMP) in the presence of divalent cations, preferably Mg2+. OMP is thereafter converted to uridine 5'-monophosphate by OMP decarboxylase. We have determined the 2.4 angstrom structure of Escherichia coli OPRTase, ligated with sulfate, by molecular replacement and refined the structure to an R-factor of 18.3% for all data. In the structure of the E. coli enzyme we have determined the fold of a flexible loop region with a highly conserved amino acid sequence among OPRTases, a region known to take part in catalysis. The structure of this region was not determined in the model used for molecular replacement, and it involves interactions at the dimer interface through a bound sulfate ion. Crystalline E. coli OPRTase is a homodimer, with sulfate ions inhibiting enzyme activity bound in the dimer interface close to the flexible loop region. Although this loop is very close in space to the sulfate binding site, and sulfate is found in both interfaces of the homodimer, the loop structure is only traceable in one monomer. We expect that the mobility of this loop is important for catalysis, and, on the basis of the reported structure and the structure of Salmonella typhimurium OPRTase.OMP, we propose that the movement of this loop in association with the movement of OMP is vital to catalysis. Apart from the flexible loop region and a solvent-exposed loop (residues 158-164), the most significant differences in structure between S. typhimurium OPRTase.OMP and E. coli OPRTase are found in the substrate binding regions: the 5'-phosphate binding region (residues 120-131), the binding region for the orotate part of OMP (residues 25-27), and the pyrophosphate binding region (residues 71-73).
<StructureSection load='1oro' size='340' side='right'caption='[[1oro]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1oro]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ORO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ORO FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1oro FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oro OCA], [https://pdbe.org/1oro PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1oro RCSB], [https://www.ebi.ac.uk/pdbsum/1oro PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1oro ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PYRE_ECOLI PYRE_ECOLI] Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP) (By similarity).<ref>PMID:8620002</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/or/1oro_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1oro ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1ORO 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=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Orotate_phosphoribosyltransferase Orotate phosphoribosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.10 2.4.2.10] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ORO OCA].
*[[Phosphoribosyltransferase 3D structures|Phosphoribosyltransferase 3D structures]]
 
== References ==
==Reference==
<references/>
A flexible loop at the dimer interface is a part of the active site of the adjacent monomer of Escherichia coli orotate phosphoribosyltransferase., Henriksen A, Aghajari N, Jensen KF, Gajhede M, Biochemistry. 1996 Mar 26;35(12):3803-9. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8620002 8620002]
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Orotate phosphoribosyltransferase]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Aghajari N]]
[[Category: Aghajari, N.]]
[[Category: Gajhede M]]
[[Category: Gajhede, M.]]
[[Category: Henriksen A]]
[[Category: Henriksen, A.]]
[[Category: Jensen KF]]
[[Category: Jensen, K F.]]
[[Category: SO4]]
[[Category: inhibitor-enzyme complex]]
[[Category: phosphoribosyltransferase]]
[[Category: pyrimidine nucleotide biosynthesis]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:20:54 2008''

Latest revision as of 11:02, 14 February 2024

A FLEXIBLE LOOP AT THE DIMER INTERFACE IS A PART OF THE ACTIVE SITE OF THE ADJACENT MONOMER OF ESCHERICHIA COLI OROTATE PHOSPHORIBOSYLTRANSFERASEA FLEXIBLE LOOP AT THE DIMER INTERFACE IS A PART OF THE ACTIVE SITE OF THE ADJACENT MONOMER OF ESCHERICHIA COLI OROTATE PHOSPHORIBOSYLTRANSFERASE

Structural highlights

1oro is a 2 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.4Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PYRE_ECOLI Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP) (By similarity).[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. ↑ Henriksen A, Aghajari N, Jensen KF, Gajhede M. A flexible loop at the dimer interface is a part of the active site of the adjacent monomer of Escherichia coli orotate phosphoribosyltransferase. Biochemistry. 1996 Mar 26;35(12):3803-9. PMID:8620002 doi:http://dx.doi.org/10.1021/bi952226y

1oro, resolution 2.40Å

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