Aspartate carbamoyltransferase: Difference between revisions

Revision as of 12:44, 11 November 2015

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 catalytic subunit contains an and a carbamoyl-phosphate-binding domain. The regulatory subunit contains a nucleotide effectors-binding domain and a zinc domain. ^[1]

Structure of E. coli aspartate carbamoyltransferase catalytic (grey 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

3D structures of aspartate carbamoyltransferase3D structures of aspartate carbamoyltransferase

Updated on 11-November-2015

ATC
- 2atc, 3at1, 6at1, 1pg5, 3d7s, 4wto – EcATC C+R subunits – Escherichia coli
- 9atc – EcATC C (mutant) + R (mutant) subunits
- 1ezz, 4e2f – EcATC C (mutant) + R subunits
- 2qg9, 2qgf – EcATC C + R (mutant) subunits
- 3csu – EcATC C
- 1gq3, 3npm – EcATC C (mutant)
- 2be7 – ATC C (mutant) + R subunits – Moritella profunda
- 2at2, 3r7d, 3r7f – BsATC – Bacillus subtilis
- 2rgw, 3e2p, 4ekn – MjATC C subunit – Methanocaldococcus jannaschii
- 3lxm – ATC C subunit – Yersinia pestis
ATC binary complex
- 1at1 – EcATC C+R subunits + malonate
- 1sku – EcATC C (mutant) +R subunits + malonate
- 1r0b – EcATC C+R subunits + citrate
- 1r0c – EcATC C+R subunits + N-carbamoyl-L-aspartate + phosphate
- 1xjw – EcATC C (mutant) +R subunits + PALA
- 1sku – EcATC C (mutant) +R subunits + phosphonoacetamide
- 1tu0 – EcATC C+R subunits + maltose
- 4at1 – EcATC C+R subunits + ATP
- 5at1, 1raa, 1rab, 1rac, 1rad, 1rae, 1raf, 1rag, 1rah, 1rai, 1za1, 4fyw – EcATC C+R subunits + CTP
- 8atc, 1acm, 1d09, 1q95 – EcATC C+R subunits + PALA
- 1f1b, 1i5o, 1tth – EcATC C (mutant) +R subunits + PALA
- 2h3e, 2ipo – EcATC C+R subunits + phosphonacetyl asparagine
- 1nbe – EcATC C (mutant) + R (mutant) subunits + malate
- 2a0f – EcATC C (mutant) +R subunits + phosphonoacetamide
- 3mpu – EcATC C (mutant) +R subunits + phosphate
- 1ekx – EcATC C + bisubstrate analog
- 1ml4 – ATC C + bisubstrate analog – Pyrococcus abyssi
- 2be9 – ATC C+R subunits + CTP – Sulfolobus acidocaldarius
- 2yww – MjATC R subunit + ATP
- 3d6n – AaATC + dihydroorotase – Aqiufex aeolicus
- 3r7l – BsATC + PALA
ATC ternary complex
- 7at1 – EcATC C+R subunits + ATP + maltose
- 8at1 – EcATC C+R subunits + CTP + maltose
- 4fyv – EcATC C+R subunits + dCTP + phosphate
- 4fyx – EcATC C+R subunits + dCTP + UTP
- 4fyy – EcATC C+R subunits + CTP + UTP
- 1za2 – EcATC C+R subunits + CTP + phosphoric monoformamide ester
- 2air – EcATC C+R subunits + L-alanosine + phosphoric monoformamide ester
- 2fzc, 2fzg – EcATC C+R subunits + CTP + phosphonic acid derivative
- 2fzk – EcATC C+R subunits + CTP + phosphonacetyl benzoate
- 4f04, 4kgv, 4kgx, 4kgz, 4kh0 – EcATC C+R subunits + nucleotide + PALA
- 2h3e – EcATC C+R subunits + phosphonacetyl asparagine + malate
- 2at1 – EcATC C+R subunits + phosphonacetamide + malate
- 2hse – EcATC C+R subunits + phosphonacetamide + aspartate
- 3d6n – AaATC + dihydroorotase + PALA
ATC quaternary complex
- 1tug – EcATC C (mutant) +R subunits + phosphate + aspartate + phosphonoacetamide
- 1tug – EcATC C (mutant) +R subunits + CTP + malonate + phosphonoacetamide
- 4kh1 – EcATC C+R subunits + UTP + CTP + phosphate + phosphonacetyl aspartate

ReferencesReferences

↑ 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

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman

[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

[1]

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 == Structural highlights ==
-ATC is composed of <scene name='59/592660/Cv/1'>2 trimers of catalytic subunits (C) and 3 dimers of regulatory subunits (R)</scene>. Click to see <scene name='59/592660/Cv/3'>two catalytic trimers</scene> and <scene name='59/592660/Cv/4'>three regulatory dimers</scene>. 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. <ref>PMID:10651286</ref>
+ATC is composed of <scene name='59/592660/Cv/1'>2 trimers of catalytic subunits (C) and 3 dimers of regulatory subunits (R)</scene>. Click to see <scene name='59/592660/Cv/3'>two catalytic trimers</scene> and <scene name='59/592660/Cv/4'>three regulatory dimers</scene>. The catalytic subunit contains an <scene name='59/592660/Cv/6'>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>