Ornithine carbamoyltransferase

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== Structural highlights ==
== Structural highlights ==
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The biological assembly of OTC is <scene name='57/573976/Cv/2'>homotrimer</scene>. OTC structure contains an <scene name='57/573976/Cv/3'>N-terminal - CP-binding domain and a C-terminal - ornithine binding domain</scene>. OCT active site is situated between the two domains<ref>PMID:18062991</ref>.
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The biological assembly of OTC is <scene name='57/573976/Cv/6'>homotrimer</scene>. OTC structure contains an <scene name='57/573976/Cv/7'>N-terminal - CP-binding domain and a C-terminal - ornithine binding domain</scene>. OCT <scene name='57/573976/Cv/8'>active site is situated between the two domains</scene><ref>PMID:18062991</ref>.
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</StructureSection>
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==3D structures of ornithine carbamoyltransferase==
==3D structures of ornithine carbamoyltransferase==
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[[Ornithine carbamoyltransferase 3D structures]]
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Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
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</StructureSection>
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{{#tree:id=OrganizedByTopic|openlevels=0|
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*Ornithine carbamoyltransferase
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**[[1a1s]], [[1pvv]] – OTC – ''Pyrococcus furiosus''<br />
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**[[2ef0]] – OTC – ''Thermus thermophilus''<br />
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**[[2p2g]] – MtOTC – ''Mycobacterium tuberculosis''<br />
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**[[3gd5]] – OTC – ''Gleobacter violaceus''<br />
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**[[3grf]] – OTC – ''Giardia intestinalis''<br />
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**[[3upd]], [[4kwt]] – VvOTC – ''Vibrio vulnificus''<br />
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**[[3sds]] – OTC – valley fever fungus<br />
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*Catabolic ornithine carbamoyltransferase
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**[[1dxh]] – PaOTC – ''Pseudomonas aeruginosa''<br />
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**[[1ort]] – PaOTC (mutant) <br />
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**[[2w37]] – OTC – ''Lactobacillus hilgardii''<br />
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**[[4amu]], [[4anf]] – OTC – ''Mycoplasma penetrans''<br />
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**[[4oh7]] – OTC – ''Brucella melitensis''<br />
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*Anabolic ornithine carbamoyltransferase
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**[[4kwt]] – VvOTC <br />
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**[[4ep1]] – BaOTC (mutant) – ''Bacillus anthracis''<br />
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**[[3tpf]] – OTC – ''Campylobacter jejuni''<br />
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**[[1akm]] – EcOTC – ''Escherichia coli''<br />
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*Ornithine carbamoyltransferase complex
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**[[1vlv]] – OTC + phosphate – ''Thermotoga maritima''<br />
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**[[2i6u]] – MtOTC + norvaline + carbamoyl phosphate <br />
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**[[4f2g]] – OTC + phosphate – ''Burkholderia thailandensis''<br />
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**[[1c9y]] – hOTC + norvaline + carbamoyl phosphate - human<br />
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**[[1ep9]], [[1fvo]] – hOTC + CP <br />
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**[[1oth]] – hOTC + ornithine derivative<br />
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**[[1duv]], [[2otc]] – EcOTC + ornithine derivative<br />
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**[[1fb5]] – sOTC + norvaline - sheep<br />
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*Anabolic ornithine carbamoyltransferase complex
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**[[4h31]] – VvOTC + norvaline + carbamoyl phosphate<br />
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**[[4jfr]] – VvOTC + carbamoyl phosphate<br />
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**[[4jhx]] – VvOTC + arginine + carbamoyl phosphate<br />
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**[[4jqo]] – VvOTC + citrulline + phosphate<br />
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**[[4nf2]] – BaOTC (mutant) + norvaline + carbamoyl phosphate<br />
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}}
 
== References ==
== References ==
<references/>
<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Current revision

Structure of ornithine carbamoyltransferase complex with carbamoyl phosphate, sulfate and the competitive inhibitor norvaline (PDB entry 2i6u)

Drag the structure with the mouse to rotate

References

  1. ↑ Murata LB, Schachman HK. Structural similarity between ornithine and aspartate transcarbamoylases of Escherichia coli: characterization of the active site and evidence for an interdomain carboxy-terminal helix in ornithine transcarbamoylase. Protein Sci. 1996 Apr;5(4):709-18. PMID:8845761 doi:http://dx.doi.org/10.1002/pro.5560050416
  2. ↑ Storkanova G, Vlaskova H, Chuzhanova N, Zeman J, Stranecky V, Majer F, Peskova K, Luksan O, Jirsa M, Hrebicek M, Dvorakova L. Ornithine carbamoyltransferase deficiency: molecular characterization of 29 families. Clin Genet. 2013 Dec;84(6):552-9. doi: 10.1111/cge.12085. Epub 2013 Feb 7. PMID:23278509 doi:http://dx.doi.org/10.1111/cge.12085
  3. ↑ Sankaranarayanan R, Cherney MM, Cherney LT, Garen CR, Moradian F, James MN. The crystal structures of ornithine carbamoyltransferase from Mycobacterium tuberculosis and its ternary complex with carbamoyl phosphate and L-norvaline reveal the enzyme's catalytic mechanism. J Mol Biol. 2008 Jan 25;375(4):1052-63. Epub 2007 Nov 19. PMID:18062991 doi:10.1016/j.jmb.2007.11.025

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky

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