1duv: Difference between revisions

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[[Image:1duv.png|left|200px]]


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==CRYSTAL STRUCTURE OF E. COLI ORNITHINE TRANSCARBAMOYLASE COMPLEXED WITH NDELTA-L-ORNITHINE-DIAMINOPHOSPHINYL-N-SULPHONIC ACID (PSORN)==
The line below this paragraph, containing "STRUCTURE_1duv", creates the "Structure Box" on the page.
<StructureSection load='1duv' size='340' side='right'caption='[[1duv]], [[Resolution|resolution]] 1.70&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'>[[1duv]] is a 3 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=1DUV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DUV FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#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=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=PSQ:NDELTA-(N-SULPHODIAMINOPHOSPHINYL)-L-ORNITHINE'>PSQ</scene></td></tr>
{{STRUCTURE_1duv| PDB=1duv |  SCENE= }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1duv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1duv OCA], [https://pdbe.org/1duv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1duv RCSB], [https://www.ebi.ac.uk/pdbsum/1duv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1duv ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/OTC1_ECOLI OTC1_ECOLI] Reversibly catalyzes the transfer of the carbamoyl group from carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine (ORN) to produce L-citrulline, which is a substrate for argininosuccinate synthetase, the enzyme involved in the final step in arginine biosynthesis.<ref>PMID:3072022</ref> <ref>PMID:789338</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/du/1duv_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=1duv ConSurf].
<div style="clear:both"></div>


===CRYSTAL STRUCTURE OF E. COLI ORNITHINE TRANSCARBAMOYLASE COMPLEXED WITH NDELTA-L-ORNITHINE-DIAMINOPHOSPHINYL-N-SULPHONIC ACID (PSORN)===
==See Also==
 
*[[Ornithine carbamoyltransferase 3D structures|Ornithine carbamoyltransferase 3D structures]]
 
== References ==
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{{ABSTRACT_PUBMED_10747936}}
 
==About this Structure==
1DUV is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DUV OCA].
 
==Reference==
Mechanism of inactivation of ornithine transcarbamoylase by Ndelta -(N'-Sulfodiaminophosphinyl)-L-ornithine, a true transition state analogue? Crystal structure and implications for catalytic mechanism., Langley DB, Templeton MD, Fields BA, Mitchell RE, Collyer CA, J Biol Chem. 2000 Jun 30;275(26):20012-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10747936 10747936]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Ornithine carbamoyltransferase]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Collyer CA]]
[[Category: Collyer, C A.]]
[[Category: Fields BA]]
[[Category: Fields, B A.]]
[[Category: Langley DB]]
[[Category: Langley, D B.]]
[[Category: Mitchell RE]]
[[Category: Mitchell, R E.]]
[[Category: Templeton MD]]
[[Category: Templeton, M D.]]
[[Category: Enzyme-inhibitor complex]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 23:39:08 2008''

Latest revision as of 09:59, 7 February 2024

CRYSTAL STRUCTURE OF E. COLI ORNITHINE TRANSCARBAMOYLASE COMPLEXED WITH NDELTA-L-ORNITHINE-DIAMINOPHOSPHINYL-N-SULPHONIC ACID (PSORN)CRYSTAL STRUCTURE OF E. COLI ORNITHINE TRANSCARBAMOYLASE COMPLEXED WITH NDELTA-L-ORNITHINE-DIAMINOPHOSPHINYL-N-SULPHONIC ACID (PSORN)

Structural highlights

1duv is a 3 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 1.7Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

OTC1_ECOLI Reversibly catalyzes the transfer of the carbamoyl group from carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine (ORN) to produce L-citrulline, which is a substrate for argininosuccinate synthetase, the enzyme involved in the final step in arginine biosynthesis.[1] [2]

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. ↑ Kuo LC, Miller AW, Lee S, Kozuma C. Site-directed mutagenesis of Escherichia coli ornithine transcarbamoylase: role of arginine-57 in substrate binding and catalysis. Biochemistry. 1988 Nov 29;27(24):8823-32. PMID:3072022
  2. ↑ Legrain C, Stalon V, Glansdorff N. Escherichia coli ornithine carbamolytransferase isoenzymes: evolutionary significance and the isolation of lambdaargF and lambdaargI transducing bacteriophages. J Bacteriol. 1976 Oct;128(1):35-8. PMID:789338

1duv, resolution 1.70Å

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