N-acetylornithine carbamoyltransferase
From Proteopedia
(Difference between revisions)
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| - | <StructureSection load='3kzn' size=' | + | <StructureSection load='3kzn' size='450' side='right' caption='N-acetylornithine carbamoyltransferase complex with acetylornithine, glycerol and sulfate (PDB code [[3kzn]]) ' scene='' pspeed='8'> |
== Function == | == Function == | ||
'''N-acetylornithine carbamoyltransferase''' (AOCT) catalyzes the reversible conversion of carbamoyl phosphate and N-acetyl-L-ornithine into N-acetyl-L-citrulline and phosphate. | '''N-acetylornithine carbamoyltransferase''' (AOCT) catalyzes the reversible conversion of carbamoyl phosphate and N-acetyl-L-ornithine into N-acetyl-L-citrulline and phosphate. | ||
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== Structural highlights == | == Structural highlights == | ||
| - | AOCT motif HCLP interacts with the produce acetyl citrulline. The substrate acetyl ornithine makes numerous H-bonds with residues in the active site of AOCT<ref>PMID:16741992</ref>. | + | AOCT motif HCLP interacts with the produce acetyl citrulline. The <scene name='75/750306/Cv/2'>substrate acetyl ornithine makes numerous H-bonds with residues in the active site of AOCT</scene><ref>PMID:16741992</ref>. Water molecules shown as red spheres. |
</StructureSection> | </StructureSection> | ||
==3D structures of N-acetylornithine carbamoyltransferase== | ==3D structures of N-acetylornithine carbamoyltransferase== | ||
Revision as of 11:00, 15 March 2017
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3D structures of N-acetylornithine carbamoyltransferase
Updated on 15-March-2017
3m4j - XcAOCT + acetyl-phosphonoacetyl ornithine - Xanthomonas campestris
3m4n, 3m5c, 3m5d - XcAOCT (mutant) + acetyl-phophonoacetyl ornithine
3kzc - XcAOCT
3kzm - XcAOCT + carbamylphosphate
3kzn - XcAOCT + acetyl ornithine
3kzo - XcAOCT + acetyl norvaline + carbamyl phosphate
3l02, 3l04, 3l05, 3l06 - XcAOCT (mutant) + norvaline derivative + carbamyl phosphate
References
- ↑ Shi D, Yu X, Roth L, Morizono H, Tuchman M, Allewell NM. Structures of N-acetylornithine transcarbamoylase from Xanthomonas campestris complexed with substrates and substrate analogs imply mechanisms for substrate binding and catalysis. Proteins. 2006 Aug 1;64(2):532-42. PMID:16741992 doi:10.1002/prot.21013
