2hls
From Proteopedia
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|PDB= 2hls |SIZE=350|CAPTION= <scene name='initialview01'>2hls</scene>, resolution 1.93Å | |PDB= 2hls |SIZE=350|CAPTION= <scene name='initialview01'>2hls</scene>, resolution 1.93Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CL:CHLORIDE ION'>CL</scene> | + | |LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2hls FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hls OCA], [http://www.ebi.ac.uk/pdbsum/2hls PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2hls RCSB]</span> | ||
}} | }} | ||
| Line 24: | Line 27: | ||
[[Category: Ambrosio, K D.]] | [[Category: Ambrosio, K D.]] | ||
[[Category: Simone, G De.]] | [[Category: Simone, G De.]] | ||
| - | [[Category: CL]] | ||
[[Category: protein disulfide oxidoreductase]] | [[Category: protein disulfide oxidoreductase]] | ||
[[Category: thioredoxin fold]] | [[Category: thioredoxin fold]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:32:06 2008'' |
Revision as of 00:32, 31 March 2008
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| , resolution 1.93Å | |||||||
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| Ligands: | |||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
The crystal structure of a protein disulfide oxidoreductase from Aeropyrum pernix k1
Overview
The formation of disulfide bonds between cysteine residues is a rate-limiting step in protein folding. To control this oxidative process, different organisms have developed different systems. In bacteria, disulfide bond formation is assisted by the Dsb protein family; in eukarya, disulfide bond formation and rearrangement are catalyzed by PDI. In thermophilic organisms, a potential key role in disulfide bond formation has recently been ascribed to a new cytosolic Protein Disulphide Oxidoreductase family whose members have a molecular mass of about 26 kDa and are characterized by two thioredoxin folds comprising a CXXC active site motif each. Here we report on the functional and structural characterization of ApPDO, a new member of this family, which was isolated from the archaeon Aeropyrum pernix K1. Functional studies have revealed that ApPDO can catalyze the reduction, oxidation and isomerization of disulfide bridges. Structural studies have shown that this protein has two CXXC active sites with fairly similar geometrical parameters typical of a stable conformation. Finally, a theoretical calculation of the cysteine pK(a) values has suggested that the two active sites have similar functional properties and each of them can impart activity to the enzyme. Our results are evidence of functional similarity between the members of the Protein Disulphide Oxidoreductase family and the eukaryotic enzyme PDI. However, as the different three-dimensional features of these two biological systems strongly suggest significantly different mechanisms of action, further experimental studies will be needed to make clear how different three-dimensional structures can result in systems with similar functional behavior.
About this Structure
2HLS is a Single protein structure of sequence from Aeropyrum pernix. Full crystallographic information is available from OCA.
Reference
A novel member of the protein disulfide oxidoreductase family from Aeropyrum pernix K1: structure, function and electrostatics., D'Ambrosio K, Pedone E, Langella E, De Simone G, Rossi M, Pedone C, Bartolucci S, J Mol Biol. 2006 Sep 29;362(4):743-52. Epub 2006 Jul 28. PMID:16934838
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