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1u11
From Proteopedia
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|PDB= 1u11 |SIZE=350|CAPTION= <scene name='initialview01'>1u11</scene>, resolution 1.55Å | |PDB= 1u11 |SIZE=350|CAPTION= <scene name='initialview01'>1u11</scene>, resolution 1.55Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CIT:CITRIC ACID'>CIT</scene> | + | |LIGAND= <scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= PurE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=435 Acetobacter aceti]) | |GENE= PurE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=435 Acetobacter aceti]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1u11 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u11 OCA], [http://www.ebi.ac.uk/pdbsum/1u11 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1u11 RCSB]</span> | ||
}} | }} | ||
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[[Category: Mill, C P.]] | [[Category: Mill, C P.]] | ||
[[Category: Settembre, E C.]] | [[Category: Settembre, E C.]] | ||
| - | [[Category: CIT]] | ||
[[Category: acidophile]] | [[Category: acidophile]] | ||
[[Category: protein stability]] | [[Category: protein stability]] | ||
[[Category: pure]] | [[Category: pure]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:03:58 2008'' |
Revision as of 21:03, 30 March 2008
| |||||||
| , resolution 1.55Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | PurE (Acetobacter aceti) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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 Mon Mar 31 00:03:58 2008
