Dihydroorotase
From Proteopedia
(Difference between revisions)
(New page: <StructureSection load='2z24' size='340' side='right' caption='Dihydroorotate complex with dihydroorotate, carbamoyl aspartate and Zn+2 ion (PDB ID 2z24)' scene=''> == Function == '...) |
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| - | + | <StructureSection load='2z24' size='340' side='right' caption='Dihydroorotate with ubunit A in grey and subunit B in green, complex with dihydroorotate, carbamoyl aspartate and Zn+2 ion (PDB ID [[2z24]])' scene=''> | |
| - | <StructureSection load='2z24' size='340' side='right' caption='Dihydroorotate complex with dihydroorotate, carbamoyl aspartate and Zn+2 ion (PDB ID [[2z24]])' scene=''> | + | |
== Function == | == Function == | ||
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== Structural highlights == | == Structural highlights == | ||
| - | The 3D structure of the complex of DHO with dihydroorotate shows | + | The 3D structure of the complex of DHO with dihydroorotate and carbamoyl aspartate shows dihydroorotate bound to the protein subunit A active site via electrostatic interactions. The substrate carbamoyl aspartate binds to the active site of subunit B via 2 Thr residues<ref>PMID:17711307</ref>. |
</StructureSection> | </StructureSection> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 06:52, 13 July 2022
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References
- ↑ Porter TN, Li Y, Raushel FM. Mechanism of the dihydroorotase reaction. Biochemistry. 2004 Dec 28;43(51):16285-92. doi: 10.1021/bi048308g. PMID:15610022 doi:http://dx.doi.org/10.1021/bi048308g
- ↑ Lee M, Maher MJ, Christopherson RI, Guss JM. Kinetic and structural analysis of mutant Escherichia coli dihydroorotases: a flexible loop stabilizes the transition state. Biochemistry. 2007 Sep 18;46(37):10538-50. Epub 2007 Aug 21. PMID:17711307 doi:10.1021/bi701098e
