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1u11

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(New page: 200px<br /><applet load="1u11" size="450" color="white" frame="true" align="right" spinBox="true" caption="1u11, resolution 1.55&Aring;" /> '''PurE (N5-carboxyamin...)
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[[Image:1u11.gif|left|200px]]<br /><applet load="1u11" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1u11.gif|left|200px]]<br /><applet load="1u11" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1u11, resolution 1.55&Aring;" />
caption="1u11, resolution 1.55&Aring;" />
'''PurE (N5-carboxyaminoimidazole Ribonucleotide Mutase) from the acidophile Acetobacter aceti'''<br />
'''PurE (N5-carboxyaminoimidazole Ribonucleotide Mutase) from the acidophile Acetobacter aceti'''<br />
==Overview==
==Overview==
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The crystal structure of Acetobacter aceti PurE was determined to a, resolution of 1.55 A and is compared with the known structures of the, class I PurEs from a mesophile, Escherichia coli, and a thermophile, Thermotoga maritima. Analyses of the general factors that increase protein, stability are examined as potential explanations for the acid stability of, A. aceti PurE. Increased inter-subunit hydrogen bonding and an increased, number of arginine-containing salt bridges appear to account for the bulk, of the increased acid stability. A chain of histidines linking two active, sites is discussed in the context of the proton transfers catalyzed by the, enzyme.
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The crystal structure of Acetobacter aceti PurE was determined to a resolution of 1.55 A and is compared with the known structures of the class I PurEs from a mesophile, Escherichia coli, and a thermophile, Thermotoga maritima. Analyses of the general factors that increase protein stability are examined as potential explanations for the acid stability of A. aceti PurE. Increased inter-subunit hydrogen bonding and an increased number of arginine-containing salt bridges appear to account for the bulk of the increased acid stability. A chain of histidines linking two active sites is discussed in the context of the proton transfers catalyzed by the enzyme.
==About this Structure==
==About this Structure==
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1U11 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Acetobacter_aceti Acetobacter aceti] with CIT as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1U11 OCA].
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1U11 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Acetobacter_aceti Acetobacter aceti] with <scene name='pdbligand=CIT:'>CIT</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U11 OCA].
==Reference==
==Reference==
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[[Category: Acetobacter aceti]]
[[Category: Acetobacter aceti]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: Chittuluru, J.R.]]
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[[Category: Chittuluru, J R.]]
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[[Category: Ealick, S.E.]]
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[[Category: Ealick, S E.]]
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[[Category: Kappock, T.J.]]
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[[Category: Kappock, T J.]]
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[[Category: Mill, C.P.]]
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[[Category: Mill, C P.]]
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[[Category: Settembre, E.C.]]
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[[Category: Settembre, E C.]]
[[Category: CIT]]
[[Category: CIT]]
[[Category: acidophile]]
[[Category: acidophile]]
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[[Category: pure]]
[[Category: pure]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 03:07:35 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:19:29 2008''

Revision as of 13:19, 21 February 2008


1u11, resolution 1.55Å

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PurE (N5-carboxyaminoimidazole Ribonucleotide Mutase) from the acidophile Acetobacter aceti

Overview

The crystal structure of Acetobacter aceti PurE was determined to a resolution of 1.55 A and is compared with the known structures of the class I PurEs from a mesophile, Escherichia coli, and a thermophile, Thermotoga maritima. Analyses of the general factors that increase protein stability are examined as potential explanations for the acid stability of A. aceti PurE. Increased inter-subunit hydrogen bonding and an increased number of arginine-containing salt bridges appear to account for the bulk of the increased acid stability. A chain of histidines linking two active sites is discussed in the context of the proton transfers catalyzed by the enzyme.

About this Structure

1U11 is a Protein complex structure of sequences from Acetobacter aceti with as ligand. Full crystallographic information is available from OCA.

Reference

Acidophilic adaptations in the structure of Acetobacter aceti N5-carboxyaminoimidazole ribonucleotide mutase (PurE)., Settembre EC, Chittuluru JR, Mill CP, Kappock TJ, Ealick SE, Acta Crystallogr D Biol Crystallogr. 2004 Oct;60(Pt 10):1753-60. Epub 2004, Sep 23. PMID:15388921

Page seeded by OCA on Thu Feb 21 15:19:29 2008

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