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1u11

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{{STRUCTURE_1u11| PDB=1u11 | SCENE= }}
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'''PurE (N5-carboxyaminoimidazole Ribonucleotide Mutase) from the acidophile Acetobacter aceti'''
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===PurE (N5-carboxyaminoimidazole Ribonucleotide Mutase) from the acidophile Acetobacter aceti===
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==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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{{ABSTRACT_PUBMED_15388921}}
==About this Structure==
==About this Structure==
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[[Category: Protein stability]]
[[Category: Protein stability]]
[[Category: Pure]]
[[Category: Pure]]
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Revision as of 07:45, 29 July 2008

Image:1u11.png

Template:STRUCTURE 1u11

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

Template:ABSTRACT PUBMED 15388921

About this Structure

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 Tue Jul 29 10:45:18 2008

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