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1d09

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[[Image:1d09.gif|left|200px]]
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{{STRUCTURE_1d09| PDB=1d09 | SCENE= }}
{{STRUCTURE_1d09| PDB=1d09 | SCENE= }}
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'''ASPARTATE TRANSCARBAMOYLASE COMPLEXED WITH N-PHOSPHONACETYL-L-ASPARTATE (PALA)'''
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===ASPARTATE TRANSCARBAMOYLASE COMPLEXED WITH N-PHOSPHONACETYL-L-ASPARTATE (PALA)===
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==Overview==
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A high-resolution structure of Escherichia coli aspartate transcarbamoylase has been determined to 2.1 A; resolution in the presence of the bisubstrate analog N-phosphonacetyl-L-aspartate (PALA). The structure was refined to a free R-factor of 23.4% and a working R-factor of 20.3%. The PALA molecule is completely saturated with interactions to side chain and backbone groups in the active site, including two interactions that are contributed from the 80s loop of the adjacent catalytic chain. The charge neutralization of the bound PALA molecule (and presumably the substrates as well) induced by the electrostatic field of the highly positively charged active site is an important factor in the high binding affinity of PALA and must be important for catalysis. The higher-resolution structure reported here departs in a number of ways from the previously determined structure at lower resolution. These modifications include alterations in the backbone conformation of the C-terminal of the catalytic chains, the N- and C-termini of the regulatory chains, and two loops of the regulatory chain. The high-resolution of this structure has allowed a more detailed description of the binding of PALA to the active site of the enzyme and has allowed a detailed model of the tetrahedral intermediate to be constructed. This model becomes the basis of a description of the catalytic mechanism of the transcarbamoylase reaction. The R-structural state of the enzyme-PALA complex is an excellent representation of the form of the enzyme that occurs at the moment in the catalytic cycle when the tetrahedral intermediate is formed. Finally, improved electron density in the N-terminal region of the regulatory chain (residues 1 to 7) has allowed tracing of the entire regulatory chain. The N-terminal segments of the R1 and R6 chains are located in close proximity to each other and to the regulatory site. This portion of the molecule may be involved in the observed asymmetry between the regulatory binding sites as well as in the heterotropic response of the enzyme.
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(as it appears on PubMed at http://www.pubmed.gov), where 10651286 is the PubMed ID number.
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{{ABSTRACT_PUBMED_10651286}}
==About this Structure==
==About this Structure==
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[[Category: Stec, B.]]
[[Category: Stec, B.]]
[[Category: Protein-inhibitor complex aspartate transcarbamoylase aspartate transcarbamylase]]
[[Category: Protein-inhibitor complex aspartate transcarbamoylase aspartate transcarbamylase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 13:18:04 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 21:55:15 2008''

Revision as of 18:55, 30 June 2008

Image:1d09.png

Template:STRUCTURE 1d09

ASPARTATE TRANSCARBAMOYLASE COMPLEXED WITH N-PHOSPHONACETYL-L-ASPARTATE (PALA)

Template:ABSTRACT PUBMED 10651286

About this Structure

1D09 is a Protein complex structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.

Reference

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., Jin L, Stec B, Lipscomb WN, Kantrowitz ER, Proteins. 1999 Dec 1;37(4):729-42. PMID:10651286

Page seeded by OCA on Mon Jun 30 21:55:15 2008

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