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| - | [[Image:1hyu.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1hyu| PDB=1hyu | SCENE= }} | | {{STRUCTURE_1hyu| PDB=1hyu | SCENE= }} |
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| - | '''CRYSTAL STRUCTURE OF INTACT AHPF'''
| + | ===CRYSTAL STRUCTURE OF INTACT AHPF=== |
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| - | ==Overview==
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| - | AhpF, a homodimer of 57 kDa subunits, is a flavoenzyme which catalyzes the NADH-dependent reduction of redox-active disulfide bonds in the peroxidase AhpC, a member of the recently identified peroxiredoxin class of antioxidant enzymes. The structure of AhpF from Salmonella typhimurium at 2.0 A resolution, determined using multiwavelength anomalous dispersion, shows that the C-terminal portion of AhpF (residues 210-521) is structurally like Escherichia coli thioredoxin reductase. In addition, AhpF has an N-terminal domain (residues 1-196) formed from two contiguous thioredoxin folds, but containing just a single redox-active disulfide (Cys129-Cys132). A flexible linker (residues 197-209) connects the domains, consistent with experiments showing that the N-terminal domain acts as an appended substrate, first being reduced by the C-terminal portion of AhpF, and subsequently reducing AhpC. Modeling studies imply that an intrasubunit electron transfer accounts for the reduction of the N-terminal domain in dimeric AhpF. Furthermore, comparing the N-terminal domain with protein disulfide oxidoreductase from Pyrococcus furiosis, we describe a new class of protein disulfide oxidoreductases based on a novel mirror-image active site arrangement, with a distinct carboxylate (Glu86) being functionally equivalent to the key acid (Asp26) of E. coli thioredoxin. A final fortuitous result is that the N-terminal redox center is reduced and provides a high-resolution view of the thiol-thiolate hydrogen bond that has been predicted to stabilize the attacking thiolate in thioredoxin-like proteins.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_11300769}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 11300769 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_11300769}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Thioredoxin]] | | [[Category: Thioredoxin]] |
| | [[Category: Thioredoxin reductase]] | | [[Category: Thioredoxin reductase]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:22:30 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 10:08:51 2008'' |
Revision as of 07:08, 1 July 2008
Template:STRUCTURE 1hyu
CRYSTAL STRUCTURE OF INTACT AHPF
Template:ABSTRACT PUBMED 11300769
About this Structure
1HYU is a Single protein structure of sequence from Salmonella typhimurium. Full crystallographic information is available from OCA.
Reference
Structure of intact AhpF reveals a mirrored thioredoxin-like active site and implies large domain rotations during catalysis., Wood ZA, Poole LB, Karplus PA, Biochemistry. 2001 Apr 3;40(13):3900-11. PMID:11300769
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