1iim: Difference between revisions

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New page: left|200px<br /><applet load="1iim" size="450" color="white" frame="true" align="right" spinBox="true" caption="1iim, resolution 2.10Å" /> '''thymidylyltransferas...
 
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[[Image:1iim.jpg|left|200px]]<br /><applet load="1iim" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1iim.jpg|left|200px]]<br /><applet load="1iim" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1iim, resolution 2.10&Aring;" />
caption="1iim, resolution 2.10&Aring;" />
'''thymidylyltransferase complexed with TTP'''<br />
'''thymidylyltransferase complexed with TTP'''<br />


==Overview==
==Overview==
Metabolite glycosylation is affected by three classes of enzymes:, nucleotidylyltransferases, which activate sugars as nucleotide, diphospho-derivatives, intermediate sugar-modifying enzymes and, glycosyltransferases, which transfer the final derivatized activated, sugars to aglycon substrates. One of the first crystal structures of an, enzyme responsible for the first step in this cascade, alpha-D-glucopyranosyl phosphate thymidylyltransferase (Ep) from, Salmonella, in complex with product (UDP-Glc) and substrate (dTTP) is, reported at 2.0 A and 2.1 A resolution, respectively. These structures, in, conjunction with the kinetic characterization of Ep, clarify the catalytic, mechanism of this important enzyme class. Structure-based engineering of, Ep produced modified enzymes capable of utilizing 'unnatural' sugar, phosphates not accepted by wild type Ep. The demonstrated ability to alter, nucleotidylyltransferase specificity by design is an integral component of, in vitro glycosylation systems developed for the production of diverse, glycorandomized libraries.
Metabolite glycosylation is affected by three classes of enzymes: nucleotidylyltransferases, which activate sugars as nucleotide diphospho-derivatives, intermediate sugar-modifying enzymes and glycosyltransferases, which transfer the final derivatized activated sugars to aglycon substrates. One of the first crystal structures of an enzyme responsible for the first step in this cascade, alpha-D-glucopyranosyl phosphate thymidylyltransferase (Ep) from Salmonella, in complex with product (UDP-Glc) and substrate (dTTP) is reported at 2.0 A and 2.1 A resolution, respectively. These structures, in conjunction with the kinetic characterization of Ep, clarify the catalytic mechanism of this important enzyme class. Structure-based engineering of Ep produced modified enzymes capable of utilizing 'unnatural' sugar phosphates not accepted by wild type Ep. The demonstrated ability to alter nucleotidylyltransferase specificity by design is an integral component of in vitro glycosylation systems developed for the production of diverse glycorandomized libraries.


==About this Structure==
==About this Structure==
1IIM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Salmonella_enterica Salmonella enterica] with TTP as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Glucose-1-phosphate_thymidylyltransferase Glucose-1-phosphate thymidylyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.24 2.7.7.24] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1IIM OCA].  
1IIM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Salmonella_enterica Salmonella enterica] with <scene name='pdbligand=TTP:'>TTP</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Glucose-1-phosphate_thymidylyltransferase Glucose-1-phosphate thymidylyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.24 2.7.7.24] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IIM OCA].  


==Reference==
==Reference==
Line 14: Line 14:
[[Category: Salmonella enterica]]
[[Category: Salmonella enterica]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Barton, W.A.]]
[[Category: Barton, W A.]]
[[Category: Biggins, J.B.]]
[[Category: Biggins, J B.]]
[[Category: Jeffrey, P.D.]]
[[Category: Jeffrey, P D.]]
[[Category: Jiang, J.]]
[[Category: Jiang, J.]]
[[Category: Lesniak, J.]]
[[Category: Lesniak, J.]]
[[Category: Nikolov, D.B.]]
[[Category: Nikolov, D B.]]
[[Category: Rajashankar, K.R.]]
[[Category: Rajashankar, K R.]]
[[Category: Thorson, J.S.]]
[[Category: Thorson, J S.]]
[[Category: TTP]]
[[Category: TTP]]
[[Category: transferase]]
[[Category: transferase]]


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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:12:15 2008''

Revision as of 14:12, 21 February 2008

File:1iim.jpg


1iim, resolution 2.10Å

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thymidylyltransferase complexed with TTP

OverviewOverview

Metabolite glycosylation is affected by three classes of enzymes: nucleotidylyltransferases, which activate sugars as nucleotide diphospho-derivatives, intermediate sugar-modifying enzymes and glycosyltransferases, which transfer the final derivatized activated sugars to aglycon substrates. One of the first crystal structures of an enzyme responsible for the first step in this cascade, alpha-D-glucopyranosyl phosphate thymidylyltransferase (Ep) from Salmonella, in complex with product (UDP-Glc) and substrate (dTTP) is reported at 2.0 A and 2.1 A resolution, respectively. These structures, in conjunction with the kinetic characterization of Ep, clarify the catalytic mechanism of this important enzyme class. Structure-based engineering of Ep produced modified enzymes capable of utilizing 'unnatural' sugar phosphates not accepted by wild type Ep. The demonstrated ability to alter nucleotidylyltransferase specificity by design is an integral component of in vitro glycosylation systems developed for the production of diverse glycorandomized libraries.

About this StructureAbout this Structure

1IIM is a Single protein structure of sequence from Salmonella enterica with as ligand. Active as Glucose-1-phosphate thymidylyltransferase, with EC number 2.7.7.24 Full crystallographic information is available from OCA.

ReferenceReference

Structure, mechanism and engineering of a nucleotidylyltransferase as a first step toward glycorandomization., Barton WA, Lesniak J, Biggins JB, Jeffrey PD, Jiang J, Rajashankar KR, Thorson JS, Nikolov DB, Nat Struct Biol. 2001 Jun;8(6):545-51. PMID:11373625

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