2fto

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(New page: 200px<br /><applet load="2fto" size="450" color="white" frame="true" align="right" spinBox="true" caption="2fto, resolution 2.00&Aring;" /> '''Y94F mutant of thymi...)
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[[Image:2fto.gif|left|200px]]<br /><applet load="2fto" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:2fto.gif|left|200px]]<br /><applet load="2fto" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2fto, resolution 2.00&Aring;" />
caption="2fto, resolution 2.00&Aring;" />
'''Y94F mutant of thymidylate synthase bound to thymidine-5'-phosphate and 10-propargyl-5,8-dideazafolid acid'''<br />
'''Y94F mutant of thymidylate synthase bound to thymidine-5'-phosphate and 10-propargyl-5,8-dideazafolid acid'''<br />
==Overview==
==Overview==
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Tyr94 of Escherichia coli thymidylate synthase is thought to be involved, either directly or by activation of a water molecule, in the abstraction, of a proton from C5 of the 2'-deoxyuridine 5'-monophosphate (dUMP), substrate. Mutation of Tyr94 leads to a 400-fold loss in catalytic, activity. The structure of the Y94F mutant has been determined in the, native state and as a ternary complex with thymidine 5'-monophosphate, (dTMP) and 10-propargyl 5,8-dideazafolate (PDDF). There are no structural, changes ascribable to the mutation other than loss of a water molecule, hydrogen bonded to the tyrosine OH, which is consistent with a catalytic, role for the phenolic OH.
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Tyr94 of Escherichia coli thymidylate synthase is thought to be involved, either directly or by activation of a water molecule, in the abstraction of a proton from C5 of the 2'-deoxyuridine 5'-monophosphate (dUMP) substrate. Mutation of Tyr94 leads to a 400-fold loss in catalytic activity. The structure of the Y94F mutant has been determined in the native state and as a ternary complex with thymidine 5'-monophosphate (dTMP) and 10-propargyl 5,8-dideazafolate (PDDF). There are no structural changes ascribable to the mutation other than loss of a water molecule hydrogen bonded to the tyrosine OH, which is consistent with a catalytic role for the phenolic OH.
==About this Structure==
==About this Structure==
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2FTO 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 PO4, TMP and CB3 as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Thymidylate_synthase Thymidylate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.45 2.1.1.45] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2FTO OCA].
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2FTO 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=PO4:'>PO4</scene>, <scene name='pdbligand=TMP:'>TMP</scene> and <scene name='pdbligand=CB3:'>CB3</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Thymidylate_synthase Thymidylate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.45 2.1.1.45] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FTO OCA].
==Reference==
==Reference==
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Structure of the Y94F mutant of Escherichia coli thymidylate synthase., Roberts SA, Hyatt DC, Honts JE, Changchien L, Maley GF, Maley F, Montfort WR, Acta Crystallograph Sect F Struct Biol Cryst Commun. 2006 Sep 1;62(Pt, 9):840-3. Epub 2006 Aug 18. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16946460 16946460]
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Structure of the Y94F mutant of Escherichia coli thymidylate synthase., Roberts SA, Hyatt DC, Honts JE, Changchien L, Maley GF, Maley F, Montfort WR, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Sep 1;62(Pt, 9):840-3. Epub 2006 Aug 18. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16946460 16946460]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Thymidylate synthase]]
[[Category: Thymidylate synthase]]
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[[Category: Montfort, W.R.]]
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[[Category: Montfort, W R.]]
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[[Category: Roberts, S.A.]]
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[[Category: Roberts, S A.]]
[[Category: CB3]]
[[Category: CB3]]
[[Category: PO4]]
[[Category: PO4]]
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[[Category: methyltransferase]]
[[Category: methyltransferase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 10:45:54 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:24:58 2008''

Revision as of 15:25, 21 February 2008


2fto, resolution 2.00Å

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Y94F mutant of thymidylate synthase bound to thymidine-5'-phosphate and 10-propargyl-5,8-dideazafolid acid

Overview

Tyr94 of Escherichia coli thymidylate synthase is thought to be involved, either directly or by activation of a water molecule, in the abstraction of a proton from C5 of the 2'-deoxyuridine 5'-monophosphate (dUMP) substrate. Mutation of Tyr94 leads to a 400-fold loss in catalytic activity. The structure of the Y94F mutant has been determined in the native state and as a ternary complex with thymidine 5'-monophosphate (dTMP) and 10-propargyl 5,8-dideazafolate (PDDF). There are no structural changes ascribable to the mutation other than loss of a water molecule hydrogen bonded to the tyrosine OH, which is consistent with a catalytic role for the phenolic OH.

About this Structure

2FTO is a Single protein structure of sequence from Escherichia coli with , and as ligands. Active as Thymidylate synthase, with EC number 2.1.1.45 Full crystallographic information is available from OCA.

Reference

Structure of the Y94F mutant of Escherichia coli thymidylate synthase., Roberts SA, Hyatt DC, Honts JE, Changchien L, Maley GF, Maley F, Montfort WR, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Sep 1;62(Pt, 9):840-3. Epub 2006 Aug 18. PMID:16946460

Page seeded by OCA on Thu Feb 21 17:24:58 2008

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