Aspartate carbamoyltransferase

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Current revision (11:16, 21 March 2019) (edit) (undo)
 
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==3D structures of aspartate carbamoyltransferase==
 
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Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
 
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{{#tree:id=OrganizedByTopic|openlevels=0|
 
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*ATC
 
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**[[2atc]], [[3at1]], [[6at1]], [[1pg5]], [[3d7s]], [[4wto]] – EcATC C+R subunits – ''Escherichia coli''<br />
 
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**[[9atc]] – EcATC C (mutant) + R (mutant) subunits <br />
 
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**[[1ezz]], [[4e2f]] – EcATC C (mutant) + R subunits <br />
 
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**[[2qg9]], [[2qgf]] – EcATC C + R (mutant) subunits <br />
 
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**[[3csu]] – EcATC C <br />
 
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**[[5vmq]], [[3npm]] – EcATC C (mutant) <br />
 
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**[[2be7]] – ATC C (mutant) + R subunits – ''Moritella profunda'' <br />
 
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**[[2at2]], [[3r7d]], [[3r7f]] – BsATC – ''Bacillus subtilis''<br />
 
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**[[2rgw]], [[3e2p]], [[4ekn]] – MjATC C subunit – ''Methanocaldococcus jannaschii''<br />
 
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**[[3lxm]] – ATC C subunit – ''Yersinia pestis''<br />
 
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**[[5ilq]], [[5iln]] – ATC – ''Plasmodium falciparum''<br />
 
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*ATC binary complex
 
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**[[1at1]] – EcATC C+R subunits + malonate<br />
 
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**[[1sku]] – EcATC C (mutant) +R subunits + malonate<br />
 
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**[[1r0b]] – EcATC C+R subunits + citrate<br />
 
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**[[1r0c]] – EcATC C+R subunits + N-carbamoyl-L-aspartate + phosphate<br />
 
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**[[1xjw]] – EcATC C (mutant) +R subunits + PALA <br />
 
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**[[1sku]] – EcATC C (mutant) +R subunits + phosphonoacetamide<br />
 
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**[[1tu0]] – EcATC C+R subunits + maltose<br />
 
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**[[4at1]] – EcATC C+R subunits + ATP<br />
 
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**[[5at1]], [[1raa]], [[1rab]], [[1rac]], [[1rad]], [[1rae]], [[1raf]], [[1rag]], [[1rah]], [[1rai]], [[1za1]], [[4fyw]] – EcATC C+R subunits + CTP<br />
 
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**[[8atc]], [[1acm]], [[1d09]], [[1q95]] – EcATC C+R subunits + PALA<br />
 
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**[[1f1b]], [[1i5o]], [[1tth]] – EcATC C (mutant) +R subunits + PALA<br />
 
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**[[2h3e]], [[2ipo]] – EcATC C+R subunits + phosphonacetyl asparagine<br />
 
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**[[1nbe]] – EcATC C (mutant) + R (mutant) subunits + malate<br />
 
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**[[2a0f]] – EcATC C (mutant) +R subunits + phosphonoacetamide<br />
 
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**[[3mpu]] – EcATC C (mutant) +R subunits + phosphate<br />
 
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**[[1ekx]] – EcATC C + bisubstrate analog<br />
 
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**[[1ml4]] – ATC C + bisubstrate analog – ''Pyrococcus abyssi''<br />
 
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**[[2be9]] – ATC C+R subunits + CTP – ''Sulfolobus acidocaldarius''<br />
 
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**[[2yww]] – MjATC R subunit + ATP <br />
 
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**[[3d6n]] – AaATC + dihydroorotase – ''Aqiufex aeolicus''<br />
 
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**[[3r7l]] – BsATC + PALA<br />
 
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*ATC ternary complex
 
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**[[7at1]] – EcATC C+R subunits + ATP + maltose<br />
 
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**[[8at1]] – EcATC C+R subunits + CTP + maltose<br />
 
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**[[4fyv]] – EcATC C+R subunits + dCTP + phosphate<br />
 
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**[[4fyx]] – EcATC C+R subunits + dCTP + UTP<br />
 
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**[[4fyy]] – EcATC C+R subunits + CTP + UTP<br />
 
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**[[1za2]] – EcATC C+R subunits + CTP + phosphoric monoformamide ester<br />
 
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**[[2air]] – EcATC C+R subunits + L-alanosine + phosphoric monoformamide ester<br />
 
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**[[2fzc]], [[2fzg]] – EcATC C+R subunits + CTP + phosphonic acid derivative<br />
 
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**[[2fzk]] – EcATC C+R subunits + CTP + phosphonacetyl benzoate<br />
 
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**[[4f04]], [[4kgv]], [[4kgx]], [[4kgz]], [[4kh0]] – EcATC C+R subunits + nucleotide + PALA<br />
 
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**[[2h3e]] – EcATC C+R subunits + phosphonacetyl asparagine + malate<br />
 
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**[[2at1]] – EcATC C+R subunits + phosphonacetamide + malate<br />
 
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**[[2hse]] – EcATC C+R subunits + phosphonacetamide + aspartate<br />
 
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**[[3d6n]], [[4bjh]] – AaATC + dihydroorotase + PALA <br />
 
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*ATC quaternary complex
 
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**[[1tug]] – EcATC C (mutant) +R subunits + phosphate + aspartate + phosphonoacetamide<br />
 
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**[[1tug]] – EcATC C (mutant) +R subunits + CTP + malonate + phosphonoacetamide<br />
 
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**[[4kh1]] – EcATC C+R subunits + UTP + CTP + phosphate + phosphonacetyl aspartate<br />
 
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}}
 
== References ==
== References ==

Current revision

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

References

  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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