Aspartate carbamoyltransferase: Difference between revisions

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<StructureSection load='1raa' size='340' side='right' caption='Structure of E. coli aspartate carbamoyltransferase catalytic (grey and pink) and regulatory (green and yellow) subunits complex with CTP (stick figure) and Zn+2 (grey) (PDB code [[1raa]]).' scene=''>
<StructureSection load='' size='350' side='right' caption='Structure of E. coli aspartate carbamoyltransferase catalytic (cyan and pink) and regulatory (green and yellow) subunits complex with inhibitor PALA and Zn+2 ions (grey) (PDB code [[1d09]]).' scene='59/592660/Cv/15'>
 
__TOC__
== Function ==
== Function ==


'''Aspartate carbamoyltransferase''' (ATC) is part of the pyrimidine biosynthesis pathway.  ATC catalyzes the condensation of aspartate and carbamoyl phosphate to N-carbamyl-L-aspartate and phosphate.  ATC is composed of 2 trimers of catalytic subunits (C) and 3 dimers of regulatory subunits (R).  The catalytic subunit contains an aspartate-binding domain and a carbamoyl-phosphate-binding domain.  The regulatory subunit contains a nucleotide effectors-binding domain and a zinc domain.  The Zn atom is essential for the association of the subunits.  Binding of the substrate to the catalytic subunits results in a high-affinity state while binding of CTP to the regulatory subunit results in a low-affinity state.  Malate and phosphonoacetyl-L-aspartate are  inhibitors of ATC.
'''Aspartate carbamoyltransferase''' (ATC) is part of the pyrimidine biosynthesis pathway.  ATC catalyzes the condensation of aspartate and carbamoyl phosphate to N-carbamyl-L-aspartate and phosphate.  The Zn atom is essential for the association of the subunits.  Binding of the substrate to the catalytic subunits results in a high-affinity state while binding of CTP to the regulatory subunit results in a low-affinity state.  Malate and phosphonoacetyl-L-aspartate (PALA) are  inhibitors of ATC.  For additional details see [[Aspartate Transcarbamoylase (ATCase)]].


== Disease ==
== Structural highlights ==
 
== Relevance ==


== Structural highlights ==
ATC is composed of <scene name='59/592660/Cv/10'>2 trimers of catalytic subunits (C) and 3 dimers of regulatory subunits (R)</scene>. Click to see <scene name='59/592660/Cv/11'>two catalytic trimers</scene> and <scene name='59/592660/Cv/12'>three regulatory dimers</scene>. The <scene name='59/592660/Cv/13'>catalytic subunit</scene> contains an <scene name='59/592660/Cv/14'>aspartate-binding domain</scene> and a carbamoyl-phosphate-binding domain.  The regulatory subunit contains a nucleotide effectors-binding domain and a zinc domain. <ref>PMID:10651286</ref>
</StructureSection>


==3D structures of aspartate carbamoyltransferase==
==3D structures of aspartate carbamoyltransferase==
[[Aspartate carbamoyltransferase 3D structures]]


Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
</StructureSection>
{{#tree:id=OrganizedByTopic|openlevels=0|
 
*ATC
 
**[[2atc]], [[3at1]], [[6at1]], [[1pg5]], [[3d7s]] – EcATC C+R subunits  – ''Escherichia coli''<br />
**[[9atc]]  – EcATC C (mutant) + R (mutant) subunits  <br />
**[[1ezz]], [[4e2f]] – EcATC C (mutant) + R subunits  <br />
**[[2qg9]], [[2qgf]]  – EcATC C + R (mutant) subunits  <br />
**[[2be7]]  – ATC C (mutant) + R subunits – ''Moritella profunda'' <br />
 
*ATC binary complex
 
**[[1at1]]  – EcATC C+R subunits  + malonate<br />
**[[1sku]]  – EcATC C (mutant) +R subunits  + malonate<br />
**[[1r0b]]  – EcATC C+R subunits  + citrate<br />
**[[1r0c]]  – EcATC C+R subunits  + N-carbamoyl-L-aspartate + phosphate<br />
**[[1xjw]]  – EcATC C (mutant) +R subunits  + phosphonacetyl-L-aspartate <br />
**[[1sku]]  – EcATC C (mutant) +R subunits  + phosphonoacetamide<br />
**[[1tu0]]  – EcATC C+R subunits  + maltose<br />
**[[4at1]]  – EcATC C+R subunits  + ATP<br />
**[[5at1]], [[1raa]], [[1rab]], [[1rac]], [[1rad]], [[1rae]], [[1raf]], [[1rag]], [[1rah]], [[1rai]], [[1za1]], [[4fyw]] – EcATC C+R subunits  + CTP<br />
**[[8atc]], [[1acm]], [[1d09]], [[1q95]] – EcATC C+R subunits  + phosphonacetyl aspartate<br />
**[[1f1b]], [[1i5o]], [[1tth]]  – EcATC C (mutant) +R subunits  + phosphonacetyl aspartate<br />
**[[2h3e]] – EcATC C+R subunits  + phosphonacetyl asparagine<br />
**[[1nbe]]  – EcATC C (mutant) + R (mutant) subunits  + malate<br />
**[[2a0f]]  – EcATC C (mutant) +R subunits + phosphonoacetamide<br />
**[[3mpu]]  – EcATC C (mutant) +R subunits + phosphate<br />
**[[2be9]] – ATC C+R subunits  + CTP – ''Sulfolobus acidocaldarius''<br />
**[[2yww]] – ATC R subunit + ATP – ''Methanocaldococcus jannaschii''<br />
 
*ATC ternary complex
 
**[[7at1]]  – EcATC C+R subunits  + ATP + maltose<br />
**[[8at1]]  – EcATC C+R subunits  + CTP + maltose<br />
**[[4fyv]]  – EcATC C+R subunits  + dCTP + phosphate<br />
**[[4fyx]]  – EcATC C+R subunits  + dCTP + UTP<br />
**[[4fyy]]  – EcATC C+R subunits  + CTP + UTP<br />
**[[1za2]]  – EcATC C+R subunits  + CTP + phosphoric monoformamide ester<br />
**[[2air]]  – EcATC C+R subunits  + L-alanosine + phosphoric monoformamide ester<br />
**[[2fzc]], [[2fzg]] – EcATC C+R subunits  + CTP + phosphonic acid derivative<br />
**[[2fzk]] – EcATC C+R subunits + CTP + phosphonacetyl benzoate<br />
**[[4f04]], [[4kgv]], [[4kgx]], [[4kgz]], [[4kh0]] – EcATC C+R subunits + nucleotide + phosphonacetyl aspartate<br />
**[[2h3e]] – EcATC C+R subunits  + phosphonacetyl asparagine + malate<br />
 
*ATC quaternary complex
 
**[[1tug]]  – EcATC C (mutant) +R subunits + phosphate + aspartate + phosphonoacetamide<br />
**[[1tug]]  – EcATC C (mutant) +R subunits + CTP + malonate + phosphonoacetamide<br />
**[[4kh1]] – EcATC C+R subunits + UTP + CTP + phosphate + phosphonacetyl aspartate<br />
 
}}


== References ==
== References ==

Latest revision as of 14:16, 21 March 2019

Function

Aspartate carbamoyltransferase (ATC) is part of the pyrimidine biosynthesis pathway. ATC catalyzes the condensation of aspartate and carbamoyl phosphate to N-carbamyl-L-aspartate and phosphate. The Zn atom is essential for the association of the subunits. Binding of the substrate to the catalytic subunits results in a high-affinity state while binding of CTP to the regulatory subunit results in a low-affinity state. Malate and phosphonoacetyl-L-aspartate (PALA) are inhibitors of ATC. For additional details see Aspartate Transcarbamoylase (ATCase).

Structural highlights

ATC is composed of . Click to see and . The contains an and a carbamoyl-phosphate-binding domain. The regulatory subunit contains a nucleotide effectors-binding domain and a zinc domain. [1]

3D structures of aspartate carbamoyltransferase

Aspartate carbamoyltransferase 3D structures


Structure of E. coli aspartate carbamoyltransferase catalytic (cyan and pink) and regulatory (green and yellow) subunits complex with inhibitor PALA and Zn+2 ions (grey) (PDB code 1d09).

Drag the structure with the mouse to rotate

ReferencesReferences

  1. ↑ Jin L, Stec B, Lipscomb WN, Kantrowitz ER. Insights into the mechanisms of catalysis and heterotropic regulation of Escherichia coli aspartate transcarbamoylase based upon a structure of the enzyme complexed with the bisubstrate analogue N-phosphonacetyl-L-aspartate at 2.1 A. Proteins. 1999 Dec 1;37(4):729-42. PMID:10651286

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Michal Harel, Alexander Berchansky, Joel L. Sussman
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