1dbr

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(New page: 200px<br /><applet load="1dbr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dbr, resolution 2.4&Aring;" /> '''HYPOXANTHINE GUANINE ...)
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[[Image:1dbr.jpg|left|200px]]<br /><applet load="1dbr" size="350" color="white" frame="true" align="right" spinBox="true"
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caption="1dbr, resolution 2.4&Aring;" />
'''HYPOXANTHINE GUANINE XANTHINE'''<br />
'''HYPOXANTHINE GUANINE XANTHINE'''<br />
==Overview==
==Overview==
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Crystal structures of substrate-free and XMP-soaked, hypoxanthine-guanine-xanthine phosphoribosyltransferase (HGXPRTase) of the, opportunistic pathogen Toxoplasma gondii have been determined to 2.4 and, 2.9 A resolution, respectively. HGXPRTase displays the conserved PRTase, fold. In the structure of the enzyme bound to its product, a long flexible, loop (residues 115-126) is located away from the active site. Comparison, to the substrate-free structure reveals a striking relocation of the loop, which is poised to cover the catalytic pocket, thus providing a mechanism, by which the HG(X)PRTases shield their oxocarbonium transition states from, nucleophilic attack by the bulk solvent. The conserved Ser 117-Tyr 118, dipeptide within the loop is brought to the active site, completing the, ensemble of catalytic residues.
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Crystal structures of substrate-free and XMP-soaked hypoxanthine-guanine-xanthine phosphoribosyltransferase (HGXPRTase) of the opportunistic pathogen Toxoplasma gondii have been determined to 2.4 and 2.9 A resolution, respectively. HGXPRTase displays the conserved PRTase fold. In the structure of the enzyme bound to its product, a long flexible loop (residues 115-126) is located away from the active site. Comparison to the substrate-free structure reveals a striking relocation of the loop, which is poised to cover the catalytic pocket, thus providing a mechanism by which the HG(X)PRTases shield their oxocarbonium transition states from nucleophilic attack by the bulk solvent. The conserved Ser 117-Tyr 118 dipeptide within the loop is brought to the active site, completing the ensemble of catalytic residues.
==About this Structure==
==About this Structure==
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1DBR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Toxoplasma_gondii Toxoplasma gondii] with MG as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DBR OCA].
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1DBR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Toxoplasma_gondii Toxoplasma gondii] with <scene name='pdbligand=MG:'>MG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DBR OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Toxoplasma gondii]]
[[Category: Toxoplasma gondii]]
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[[Category: Brennan, R.G.]]
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[[Category: Brennan, R G.]]
[[Category: Carter, D.]]
[[Category: Carter, D.]]
[[Category: Roos, D.]]
[[Category: Roos, D.]]
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[[Category: Schumacher, M.A.]]
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[[Category: Schumacher, M A.]]
[[Category: Ullman, B.]]
[[Category: Ullman, B.]]
[[Category: MG]]
[[Category: MG]]
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[[Category: transferase]]
[[Category: transferase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:08:41 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:14:58 2008''

Revision as of 10:15, 21 February 2008


1dbr, resolution 2.4Å

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HYPOXANTHINE GUANINE XANTHINE

Overview

Crystal structures of substrate-free and XMP-soaked hypoxanthine-guanine-xanthine phosphoribosyltransferase (HGXPRTase) of the opportunistic pathogen Toxoplasma gondii have been determined to 2.4 and 2.9 A resolution, respectively. HGXPRTase displays the conserved PRTase fold. In the structure of the enzyme bound to its product, a long flexible loop (residues 115-126) is located away from the active site. Comparison to the substrate-free structure reveals a striking relocation of the loop, which is poised to cover the catalytic pocket, thus providing a mechanism by which the HG(X)PRTases shield their oxocarbonium transition states from nucleophilic attack by the bulk solvent. The conserved Ser 117-Tyr 118 dipeptide within the loop is brought to the active site, completing the ensemble of catalytic residues.

About this Structure

1DBR is a Single protein structure of sequence from Toxoplasma gondii with as ligand. Full crystallographic information is available from OCA.

Reference

Crystal structures of Toxoplasma gondii HGXPRTase reveal the catalytic role of a long flexible loop., Schumacher MA, Carter D, Ross DS, Ullman B, Brennan RG, Nat Struct Biol. 1996 Oct;3(10):881-7. PMID:8836106

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