1hyu
From Proteopedia
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|PDB= 1hyu |SIZE=350|CAPTION= <scene name='initialview01'>1hyu</scene>, resolution 2.00Å | |PDB= 1hyu |SIZE=350|CAPTION= <scene name='initialview01'>1hyu</scene>, resolution 2.00Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hyu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hyu OCA], [http://www.ebi.ac.uk/pdbsum/1hyu PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1hyu RCSB]</span> | ||
}} | }} | ||
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[[Category: Poole, L B.]] | [[Category: Poole, L B.]] | ||
[[Category: Wood, Z A.]] | [[Category: Wood, Z A.]] | ||
| - | [[Category: CL]] | ||
| - | [[Category: FAD]] | ||
| - | [[Category: SO4]] | ||
[[Category: nucleotide binding fold]] | [[Category: nucleotide binding fold]] | ||
[[Category: thiol-thiolate hydrogen bond]] | [[Category: thiol-thiolate hydrogen bond]] | ||
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[[Category: thioredoxin reductase]] | [[Category: thioredoxin reductase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:12:11 2008'' |
Revision as of 18:12, 30 March 2008
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| , resolution 2.00Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF INTACT AHPF
Overview
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.
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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