Structure of N5-carboxyaminoimidazole
ribonucleotide synthase (PurK) from Bacillus
anthracis
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| Title: |
Structure of N5-carboxyaminoimidazole
ribonucleotide synthase (PurK) from Bacillus
anthracis |
| Author(s): |
Tuntland, M. L.; Johnson, M. E.; Fung, L.; Santarsiero, B. D.
|
| Abstract: |
The apo structure of N5-carboxyaminoimidazole ribonucleotide synthase (PurK) from Bacillus anthracis (baPurK) with Mg2+ in the active site is reported at 1.96 A ° resolution. PurK
is an enzyme in the purine-biosynthetic pathway, unique to prokaryotes, that converts 5-aminoimidazole ribonucleotide to N5-carboxyaminoimidazole ribonucleotide and has been suggested as a potential antimicrobial drug target. Two interesting features of baPurK are a flexible B-loop (residues
149/150–157) that is in close contact with the active site and the binding of Mg2+ to the active site without additional ligands. |
| Issue Date: |
2011-10 |
| Publisher: |
International Union of Crystallography |
| Citation Info: |
Tuntland, M. L., Johnson, M. E., Fung, L., & Santarsiero, B. D. 2011. Structure of N(5)-carboxyaminoimidazole ribonucleotide synthase (PurK) from Bacillus anthracis. Acta Crystallographica Section D-Biological Crystallography, 67: 870-874. DOI: 10.1107/S0907444911029210 |
| Type: |
Article |
| Description: |
This is a copy of an article published in the Acta Crystallographica Section D-Biological Crystallography © 2011 International Union of Crystallography. DOI: 10.1107/S0907444911029210 |
| URI: |
http://hdl.handle.net/10027/8169
|
| ISSN: |
0907-4449 |
| Date Available in INDIGO: |
2012-03-06 |
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