Aspartate carbamoyltransferase

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Line 28: Line 28:
**[[2rgw]], [[3e2p]], [[4ekn]] – MjATC C subunit – ''Methanocaldococcus jannaschii''<br />
**[[2rgw]], [[3e2p]], [[4ekn]] – MjATC C subunit – ''Methanocaldococcus jannaschii''<br />
**[[3lxm]] – ATC C subunit – ''Yersinia pestis''<br />
**[[3lxm]] – ATC C subunit – ''Yersinia pestis''<br />
 +
**[[5ilq]] – ATC – ''Plasmodium falciparum''<br />
*ATC binary complex
*ATC binary complex
Line 68: Line 69:
**[[2at1]] – EcATC C+R subunits + phosphonacetamide + malate<br />
**[[2at1]] – EcATC C+R subunits + phosphonacetamide + malate<br />
**[[2hse]] – EcATC C+R subunits + phosphonacetamide + aspartate<br />
**[[2hse]] – EcATC C+R subunits + phosphonacetamide + aspartate<br />
-
**[[3d6n]] – AaATC + dihydroorotase + PALA <br />
+
**[[3d6n]], [[4bjh]] – AaATC + dihydroorotase + PALA <br />
*ATC quaternary complex
*ATC quaternary complex

Revision as of 10:53, 12 March 2017

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 carbamoyltransferase

Updated on 12-March-2017

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

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman

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