1opr: Difference between revisions

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[[Image:1opr.jpg|left|200px]]


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==THE CRYSTAL STRUCTURE OF THE OROTATE PHOSPHORIBOSYLTRANSFERASE COMPLEXED WITH OROTATE AND ALPHA-D-5-PHOSPHORIBOSYL-1-PYROPHOSPHATE==
The line below this paragraph, containing "STRUCTURE_1opr", creates the "Structure Box" on the page.
<StructureSection load='1opr' size='340' side='right'caption='[[1opr]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1opr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_Typhimurium Salmonella enterica subsp. enterica serovar Typhimurium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OPR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OPR FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ORO:OROTIC+ACID'>ORO</scene>, <scene name='pdbligand=PRP:ALPHA-PHOSPHORIBOSYLPYROPHOSPHORIC+ACID'>PRP</scene></td></tr>
{{STRUCTURE_1opr| PDB=1opr |  SCENE= }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1opr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1opr OCA], [https://pdbe.org/1opr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1opr RCSB], [https://www.ebi.ac.uk/pdbsum/1opr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1opr ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PYRE_SALTY PYRE_SALTY] 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:2271660</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/op/1opr_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=1opr ConSurf].
<div style="clear:both"></div>


'''THE CRYSTAL STRUCTURE OF THE OROTATE PHOSPHORIBOSYLTRANSFERASE COMPLEXED WITH OROTATE AND ALPHA-D-5-PHOSPHORIBOSYL-1-PYROPHOSPHATE'''
==See Also==
 
*[[Phosphoribosyltransferase 3D structures|Phosphoribosyltransferase 3D structures]]
 
== References ==
==Overview==
<references/>
The three-dimensional structure of Salmonella typhimurium orotate phosphoribosyltransferase (OPRTase) in complex with the ribose 5-phosphate donor alpha-D-5--phosphoribosyl-1-pyrophosphate (PRPP) and the nitrogenous base orotic acid has been solved and refined with X-ray diffraction data extending to 2.3 A resolution to a crystallographic R-factor of 18.7%. The complex was generated by carrying out catalysis in the crystal. Comparison of this structure with the previously reported structure of the orotidine 5'-monophosphate (OMP) complex [Scapin, G., Grubmeyer, C., and Sacchettini, J. C. (1994) Biochemistry 33, 1287-1294] revealed that the enzyme backbone undergoes only small movements. The most significant differences occur near the active site, at Ala71-Gly74, with the largest difference involving the side chains of Lys73, Val127-Ala133, the 5'-phosphate binding loop, and a long, solvent-exposed loop at the dimer interface. The position of the ribose moiety is, on the other hand, very different in the OMP and PRPP.orotate complexes, with its anomeric carbon moving approximately 7 A across the binding cavity. In the PRPP.orotate complex the highly conserved acidic side chain of Asp124 interacts with the ribose of PRPP, whereas there are no interactions of this aspartate with the substrate in the OMP complex.
__TOC__
 
</StructureSection>
==About this Structure==
[[Category: Large Structures]]
1OPR is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Salmonella_typhimurium Salmonella typhimurium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OPR OCA].
[[Category: Salmonella enterica subsp. enterica serovar Typhimurium]]
 
[[Category: Sacchettini JC]]
==Reference==
[[Category: Scapin G]]
The crystal structure of the orotate phosphoribosyltransferase complexed with orotate and alpha-D-5-phosphoribosyl-1-pyrophosphate., Scapin G, Ozturk DH, Grubmeyer C, Sacchettini JC, Biochemistry. 1995 Aug 29;34(34):10744-54. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7545004 7545004]
[[Category: Orotate phosphoribosyltransferase]]
[[Category: Salmonella typhimurium]]
[[Category: Single protein]]
[[Category: Sacchettini, J C.]]
[[Category: Scapin, G.]]
[[Category: Transferase]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 04:08:21 2008''

Latest revision as of 11:02, 14 February 2024

THE CRYSTAL STRUCTURE OF THE OROTATE PHOSPHORIBOSYLTRANSFERASE COMPLEXED WITH OROTATE AND ALPHA-D-5-PHOSPHORIBOSYL-1-PYROPHOSPHATETHE CRYSTAL STRUCTURE OF THE OROTATE PHOSPHORIBOSYLTRANSFERASE COMPLEXED WITH OROTATE AND ALPHA-D-5-PHOSPHORIBOSYL-1-PYROPHOSPHATE

Structural highlights

1opr is a 1 chain structure with sequence from Salmonella enterica subsp. enterica serovar Typhimurium. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.3Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PYRE_SALTY 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. ↑ Bhatia MB, Vinitsky A, Grubmeyer C. Kinetic mechanism of orotate phosphoribosyltransferase from Salmonella typhimurium. Biochemistry. 1990 Nov 20;29(46):10480-7. PMID:2271660

1opr, resolution 2.30Å

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