2h1a
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= resA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 Bacillus subtilis]) | |GENE= resA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 Bacillus subtilis]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1su9|1SU9]], [[1st9|1ST9]], [[2h19|2H19]], [[2h1b|2H1B]], [[2h1d|2H1D]], [[2h1g|2H1G]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2h1a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h1a OCA], [http://www.ebi.ac.uk/pdbsum/2h1a PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2h1a RCSB]</span> | ||
}} | }} | ||
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[[Category: Lewin, A.]] | [[Category: Lewin, A.]] | ||
[[Category: Oubrie, A.]] | [[Category: Oubrie, A.]] | ||
| - | [[Category: EDO]] | ||
[[Category: c74a]] | [[Category: c74a]] | ||
[[Category: mutant]] | [[Category: mutant]] | ||
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[[Category: variant]] | [[Category: variant]] | ||
| - | ''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 03:24:03 2008'' |
Revision as of 00:24, 31 March 2008
| |||||||
| , resolution 2.400Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | resA (Bacillus subtilis) | ||||||
| Related: | 1SU9, 1ST9, 2H19, 2H1B, 2H1D, 2H1G
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
ResA C74A Variant
Overview
ResA, an extracytoplasmic thioredoxin from Bacillus subtilis, acts in cytochrome c maturation by reducing the disulfide bond present in apocytochromes prior to covalent attachment of heme. This reaction is (and has to be) specific, as broad substrate specificity would result in unproductive shortcircuiting with the general oxidizing thioredoxin(s) present in the same compartment. Using mutational analysis and subsequent biochemical and structural characterization of active site variants, we show that reduced ResA displays unusually low reactivity at neutral pH, consistent with the observed high pKa values>8 for both active site cysteines. Residue Glu80 is shown to play a key role in controlling the acid-base properties of the active site. A model in which substrate binding dramatically enhances the reactivity of the active site cysteines is proposed to account for the specificity of the protein. Such a substratemediated activation mechanism is likely to have wide relevance for extracytoplasmic thioredoxins.
About this Structure
2H1A is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.
Reference
Molecular basis for specificity of the extracytoplasmic thioredoxin ResA., Lewin A, Crow A, Oubrie A, Le Brun NE, J Biol Chem. 2006 Nov 17;281(46):35467-77. Epub 2006 Sep 13. PMID:16971393
Page seeded by OCA on Mon Mar 31 03:24:03 2008
Categories: Bacillus subtilis | Single protein | Brun, N E.Le. | Crow, A. | Lewin, A. | Oubrie, A. | C74a | Mutant | Resa | Thioredoxin | Variant
