1akm: Difference between revisions

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


{{STRUCTURE_1akm| PDB=1akm | SCENE= }}
==ORNITHINE TRANSCARBAMYLASE FROM ESCHERICHIA COLI==
<StructureSection load='1akm' size='340' side='right'caption='[[1akm]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1akm]] 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=1AKM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AKM 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]] 2.8&#8491;</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=1akm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1akm OCA], [https://pdbe.org/1akm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1akm RCSB], [https://www.ebi.ac.uk/pdbsum/1akm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1akm 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/ak/1akm_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=1akm ConSurf].
<div style="clear:both"></div>


===ORNITHINE TRANSCARBAMYLASE FROM ESCHERICHIA COLI===
==See Also==
 
*[[Ornithine carbamoyltransferase 3D structures|Ornithine carbamoyltransferase 3D structures]]
 
== References ==
==About this Structure==
<references/>
[[1akm]] is a 3 chain structure with 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=1AKM OCA].
__TOC__
 
</StructureSection>
==Reference==
<ref group="xtra">PMID:009253409</ref><references group="xtra"/>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Ornithine carbamoyltransferase]]
[[Category: Large Structures]]
[[Category: Head, J F.]]
[[Category: Head JF]]
[[Category: Jin, L.]]
[[Category: Jin L]]
[[Category: Seaton, B.]]
[[Category: Seaton B]]
[[Category: Anabolic]]
[[Category: Carbamyl phosphate]]
[[Category: Transferase]]
[[Category: Urea cycle]]

Latest revision as of 13:53, 2 August 2023

ORNITHINE TRANSCARBAMYLASE FROM ESCHERICHIA COLIORNITHINE TRANSCARBAMYLASE FROM ESCHERICHIA COLI

Structural highlights

1akm 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 2.8Å
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

1akm, resolution 2.80Å

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