Structural highlights
Function
[PYRI_ECOLI] Involved in allosteric regulation of aspartate carbamoyltransferase.[HAMAP-Rule:MF_00002]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The structure of aspartate transcarbamylase of Escherichia coli ligated to products (phosphate and N-carbamyl-l-aspartate) has been determined at 2.37 A resolution (R-factor = 0.23, R(free) = 0.27). Results might indicate a product release mode, rather than close analogues to the transition state like those found in our earlier studies of other ligands (N-phosphonacetyl-L-aspartate, carbamyl phosphate plus malonate, phosphonoacetamide plus malonate, or citrate plus phosphate). Ordered product release, first carbamylaspartate (CLA) and then phosphate, might be facilitated by a 4 A movement of phosphate from the substrate-analogue position to the product (phosphate) binding position, and by a somewhat similar release movement of the other product (CLA) relative to its analogue (citrate). This movement is consistent with earlier studies of binding of either pyrophosphate or phosphate alone [Honzatko, R. B., and Lipscomb, W. N. (1982) J. Mol. Biol. 160, 265-286].
Products in the T-state of aspartate transcarbamylase: crystal structure of the phosphate and N-carbamyl-L-aspartate ligated enzyme.,Huang J, Lipscomb WN Biochemistry. 2004 Jun 1;43(21):6422-6. PMID:15157076[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Huang J, Lipscomb WN. Products in the T-state of aspartate transcarbamylase: crystal structure of the phosphate and N-carbamyl-L-aspartate ligated enzyme. Biochemistry. 2004 Jun 1;43(21):6422-6. PMID:15157076 doi:10.1021/bi0302144
