This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1jqc
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:1jqc.jpg|left|200px]] | + | [[Image:1jqc.jpg|left|200px]] |
| - | + | ||
| - | '''Mn substituted Ribonucleotide reductase R2 from E. Coli oxidized by hydrogen peroxide and hydroxylamine''' | + | {{Structure |
| + | |PDB= 1jqc |SIZE=350|CAPTION= <scene name='initialview01'>1jqc</scene>, resolution 1.61Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene> and <scene name='pdbligand=HG:MERCURY (II) ION'>HG</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Ribonucleoside-diphosphate_reductase Ribonucleoside-diphosphate reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.17.4.1 1.17.4.1] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''Mn substituted Ribonucleotide reductase R2 from E. Coli oxidized by hydrogen peroxide and hydroxylamine''' | ||
| + | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1JQC is a [ | + | 1JQC is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JQC OCA]. |
==Reference== | ==Reference== | ||
| - | Crystal structures of oxidized dinuclear manganese centres in Mn-substituted class I ribonucleotide reductase from Escherichia coli: carboxylate shifts with implications for O2 activation and radical generation., Hogbom M, Andersson ME, Nordlund P, J Biol Inorg Chem. 2001 Mar;6(3):315-23. PMID:[http:// | + | Crystal structures of oxidized dinuclear manganese centres in Mn-substituted class I ribonucleotide reductase from Escherichia coli: carboxylate shifts with implications for O2 activation and radical generation., Hogbom M, Andersson ME, Nordlund P, J Biol Inorg Chem. 2001 Mar;6(3):315-23. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11315567 11315567] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Ribonucleoside-diphosphate reductase]] | [[Category: Ribonucleoside-diphosphate reductase]] | ||
| Line 24: | Line 33: | ||
[[Category: ribonucleotide reductase r2]] | [[Category: ribonucleotide reductase r2]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:06:57 2008'' |
Revision as of 10:06, 20 March 2008
| |||||||
| , resolution 1.61Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Activity: | Ribonucleoside-diphosphate reductase, with EC number 1.17.4.1 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Mn substituted Ribonucleotide reductase R2 from E. Coli oxidized by hydrogen peroxide and hydroxylamine
Overview
The di-iron carboxylate proteins constitute a diverse class of non-heme iron enzymes performing a multitude of redox reactions. These reactions usually involve high-valent Fe-oxo species and are thought to be controlled by carboxylate shifts. Owing to their short lifetime, the intermediate structures have so far escaped structural characterization by X-ray crystallography. In an attempt to map the carboxylate conformations available to the protein during different redox states and different ligand environments, we have studied metal-substituted forms of the R2 protein of ribonucleotide reductase from Escherichia coli. In the present work we have solved the crystal structures of Mn-substituted R2 oxidized in two different ways. Oxidation was performed using either nitric oxide or a combination of hydrogen peroxide and hydroxylamine. The two structures are virtually identical, indicating that the oxidation states are the same, most likely a mixed-valent MnII-MnIII centre. One of the carboxylate ligands (D84) adopts a new, so far unseen, conformation, which could participate in the mechanism for radical generation in R2. E238 adopts a bridging-chelating conformation proposed to be important for proper O2 activation but not previously observed in the wild-type enzyme. Probable catalase activity was also observed during the oxidation with H2O2, indicating mechanistic similarities to the di-Mn catalases.
About this Structure
1JQC is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Crystal structures of oxidized dinuclear manganese centres in Mn-substituted class I ribonucleotide reductase from Escherichia coli: carboxylate shifts with implications for O2 activation and radical generation., Hogbom M, Andersson ME, Nordlund P, J Biol Inorg Chem. 2001 Mar;6(3):315-23. PMID:11315567
Page seeded by OCA on Thu Mar 20 12:06:57 2008
