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| - | [[Image:1qxh.jpg|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1qxh| PDB=1qxh | SCENE= }} | | {{STRUCTURE_1qxh| PDB=1qxh | SCENE= }} |
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| - | '''Crystal Structure of Escherichia coli Thiol Peroxidase in the Oxidized State'''
| + | ===Crystal Structure of Escherichia coli Thiol Peroxidase in the Oxidized State=== |
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| - | ==Overview==
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| - | Thioredoxin-dependent thiol peroxidase (Tpx) from Escherichia coli represents a group of antioxidant enzymes that are widely distributed in pathogenic bacterial species and which belong to the peroxiredoxin (Prx) family. Bacterial Tpxs are unique in that the location of the resolving cysteine (CR) is different from those of other Prxs. E. coli Tpx (EcTpx) shows substrate specificity toward alkyl hydroperoxides over H2O2 and is the most potent reductant of alkyl hydroperoxides surpassing AhpC and BCP, the other E. coli Prx members. Here, we present the crystal structure of EcTpx in the oxidized state determined at 2.2-A resolution. The structure revealed that Tpxs are the second type of atypical 2-Cys Prxs with an intramolecular disulfide bond formed between the peroxidatic (CP, Cys61) and resolving (Cys95) cysteine residues. The extraordinarily long N-terminal chain of EcTpx folds into a beta-hairpin making the overall structure very compact. Modeling suggests that, in atypical 2-Cys Prxs, the CR-loop as well as the CP-loop may alternately assume the fully folded or locally unfolded conformation depending on redox states, as does the CP-loop in typical 2-Cys Prxs. EcTpx exists as a dimer stabilized by hydrogen bonds. Its substrate binding site extends to the dimer interface. A modeled structure of the reduced EcTpx in complex with 15-hydroperoxyeicosatetraenoic acid suggests that the size and shape of the binding site are particularly suited for long fatty acid hydroperoxides consistent with its greater reactivity.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_14506251}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 14506251 is the PubMed ID number. |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Scavengase p20]] | | [[Category: Scavengase p20]] |
| | [[Category: Thiol peroxidase]] | | [[Category: Thiol peroxidase]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:49:12 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 19:48:41 2008'' |
Revision as of 16:48, 28 July 2008
Template:STRUCTURE 1qxh
Crystal Structure of Escherichia coli Thiol Peroxidase in the Oxidized State
Template:ABSTRACT PUBMED 14506251
About this Structure
1QXH is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Crystal structure of Escherichia coli thiol peroxidase in the oxidized state: insights into intramolecular disulfide formation and substrate binding in atypical 2-Cys peroxiredoxins., Choi J, Choi S, Choi J, Cha MK, Kim IH, Shin W, J Biol Chem. 2003 Dec 5;278(49):49478-86. Epub 2003 Sep 23. PMID:14506251
Page seeded by OCA on Mon Jul 28 19:48:41 2008
