Ornithine carbamoyltransferase

From Proteopedia

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spinqualitylabelsall models Structure of ornithine carbamoyltransferase complex with carbamoyl phosphate and the competitive inhibitor norvaline (PDB entry 2i6u) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Function Ornithine carbamoyltransferase (OTC) catalyzes the conversion of carbamoyl phosphate and ornithine to citrulline and phosphate. OTC is part of the arginine biosynthesis in plants and bacteria and part of the urea cycle in mammals[1]. For details see Sanbox Reserved 684. Disease OCT deficiency is a genetic urea cycle disorder. Structural highlights

3D structures of ornithine carbamoyltransferase

Updated on 09-June-2016

1a1s, 1pvv – OTC – Pyrococcus furiosus
2ef0 – OTC – Thermus thermophilus
2p2g – MtOTC – Mycobacterium tuberculosis
3gd5 – OTC – Gleobacter violaceus
3grf – OTC – Giardia intestinalis
3tpf – OTC – Campylobacter jejuni
3upd, 4kwt – VvOTC – Vibrio vulnificus
4ep1 – BaOTC (mutant) – Bacillus anthracis
1akm – EcOTC – Escherichia coli
1dxh – PaOTC – Pseudomonas aeruginosa
1ort – PaOTC (mutant)
2w37 – OTC – Lactobacillus hilgardii
3sds – OTC – valley fever fungus
4amu, 4anf – OTC – Mycoplasma penetrans
4oh7 – OTC – Brucella melitensis

Ornithine carbamoyltransferase complex

1vlv – OTC + phosphate – Thermotoga maritima
2i6u – MtOTC + norvaline + carbamoyl phosphate
4f2g – OTC + phosphate – Burkholderia thailandensis
4h31 – VvOTC + norvaline + carbamoyl phosphate
4jfr – VvOTC + carbamoyl phosphate
4jhx – VvOTC + arginine + carbamoyl phosphate
4jqo – VvOTC + citrulline + phosphate
4nf2 – BaOTC (mutant) + norvaline + carbamoyl phosphate
1c9y – hOTC + norvaline + carbamoyl phosphate - human
1ep9, 1fvo – hOTC + carbamoyl phosphate
1oth – hOTC + ornithine derivative
1duv, 2otc – EcOTC + ornithine derivative
1fb5 – sOTC + norvaline - sheep

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