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New page: left|200px<br /><applet load="1duv" size="450" color="white" frame="true" align="right" spinBox="true" caption="1duv, resolution 1.7Å" /> '''CRYSTAL STRUCTURE OF ...
 
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[[Image:1duv.jpg|left|200px]]<br /><applet load="1duv" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1duv.jpg|left|200px]]<br /><applet load="1duv" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1duv, resolution 1.7&Aring;" />
caption="1duv, resolution 1.7&Aring;" />
'''CRYSTAL STRUCTURE OF E. COLI ORNITHINE TRANSCARBAMOYLASE COMPLEXED WITH NDELTA-L-ORNITHINE-DIAMINOPHOSPHINYL-N-SULPHONIC ACID (PSORN)'''<br />
'''CRYSTAL STRUCTURE OF E. COLI ORNITHINE TRANSCARBAMOYLASE COMPLEXED WITH NDELTA-L-ORNITHINE-DIAMINOPHOSPHINYL-N-SULPHONIC ACID (PSORN)'''<br />


==Overview==
==Overview==
The crystal structure is reported at 1.8 A resolution of Escherichia coli, ornithine transcarbamoylase in complex with the active derivative of, phaseolotoxin from Pseudomonas syringae pv. phaseolicola, N(delta)-(N'-sulfodiaminophosphinyl)-l-ornithine. Electron density reveals, that the complex is not a covalent adduct as previously thought. Kinetic, data confirm that N(delta)-(N'-sulfodiaminophosphinyl)-l-ornithine, exhibits reversible inhibition with a half-life in the order of, approximately 22 h and a dissociation constant of K(D) = 1.6 x 10(-12) m, at 37 degrees C and pH 8.0. Observed hydrogen bonding about the chiral, tetrahedral phosphorus of the inhibitor is consistent only with the, presence of the R enantiomer. A strong interaction is also observed, between Arg(57) Nepsilon and the P-N-S bridging nitrogen indicating that, imino tautomers of N(delta)-(N'-sulfodiaminophosphinyl)-l-ornithine are, present in the bound state. An imino tautomer of, N(delta)-(N'-sulfodiaminophosphinyl)-l-ornithine is structurally analogous, to the proposed reaction transition state. Hence, we propose that, N(delta)-(N'-sulfodiaminophosphinyl)-l-ornithine, with its three unique, N-P bonds, represents a true transition state analogue for ornithine, transcarbamoylases, consistent with the tight binding kinetics observed.
The crystal structure is reported at 1.8 A resolution of Escherichia coli ornithine transcarbamoylase in complex with the active derivative of phaseolotoxin from Pseudomonas syringae pv. phaseolicola, N(delta)-(N'-sulfodiaminophosphinyl)-l-ornithine. Electron density reveals that the complex is not a covalent adduct as previously thought. Kinetic data confirm that N(delta)-(N'-sulfodiaminophosphinyl)-l-ornithine exhibits reversible inhibition with a half-life in the order of approximately 22 h and a dissociation constant of K(D) = 1.6 x 10(-12) m at 37 degrees C and pH 8.0. Observed hydrogen bonding about the chiral tetrahedral phosphorus of the inhibitor is consistent only with the presence of the R enantiomer. A strong interaction is also observed between Arg(57) Nepsilon and the P-N-S bridging nitrogen indicating that imino tautomers of N(delta)-(N'-sulfodiaminophosphinyl)-l-ornithine are present in the bound state. An imino tautomer of N(delta)-(N'-sulfodiaminophosphinyl)-l-ornithine is structurally analogous to the proposed reaction transition state. Hence, we propose that N(delta)-(N'-sulfodiaminophosphinyl)-l-ornithine, with its three unique N-P bonds, represents a true transition state analogue for ornithine transcarbamoylases, consistent with the tight binding kinetics observed.


==About this Structure==
==About this Structure==
1DUV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with PSQ and MPD as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Ornithine_carbamoyltransferase Ornithine carbamoyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.3.3 2.1.3.3] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DUV OCA].  
1DUV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=PSQ:'>PSQ</scene> and <scene name='pdbligand=MPD:'>MPD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Ornithine_carbamoyltransferase Ornithine carbamoyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.3.3 2.1.3.3] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DUV OCA].  


==Reference==
==Reference==
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[[Category: Ornithine carbamoyltransferase]]
[[Category: Ornithine carbamoyltransferase]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Collyer, C.A.]]
[[Category: Collyer, C A.]]
[[Category: Fields, B.A.]]
[[Category: Fields, B A.]]
[[Category: Langley, D.B.]]
[[Category: Langley, D B.]]
[[Category: Mitchell, R.E.]]
[[Category: Mitchell, R E.]]
[[Category: Templeton, M.D.]]
[[Category: Templeton, M D.]]
[[Category: MPD]]
[[Category: MPD]]
[[Category: PSQ]]
[[Category: PSQ]]
[[Category: enzyme-inhibitor complex]]
[[Category: enzyme-inhibitor complex]]


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