1ti1
From Proteopedia
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|LIGAND= <scene name='pdbligand=D12:DODECANE'>D12</scene> | |LIGAND= <scene name='pdbligand=D12:DODECANE'>D12</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
| - | |GENE= DSBA, PPFA, DSF, B3860, Z5392, ECS4783 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id= | + | |GENE= DSBA, PPFA, DSF, B3860, Z5392, ECS4783 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83334 Escherichia coli O157:H7]) |
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1dsb|1DSB]], [[1fvk|1FVK]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ti1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ti1 OCA], [http://www.ebi.ac.uk/pdbsum/1ti1 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ti1 RCSB]</span> | ||
}} | }} | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1TI1 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ | + | 1TI1 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_o157:h7 Escherichia coli o157:h7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TI1 OCA]. |
==Reference== | ==Reference== | ||
Intriguing conformation changes associated with the trans/cis isomerization of a prolyl residue in the active site of the DsbA C33A mutant., Ondo-Mbele E, Vives C, Kone A, Serre L, J Mol Biol. 2005 Apr 1;347(3):555-63. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15755450 15755450] | Intriguing conformation changes associated with the trans/cis isomerization of a prolyl residue in the active site of the DsbA C33A mutant., Ondo-Mbele E, Vives C, Kone A, Serre L, J Mol Biol. 2005 Apr 1;347(3):555-63. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15755450 15755450] | ||
| - | [[Category: Escherichia coli | + | [[Category: Escherichia coli o157:h7]] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Kone, A.]] | [[Category: Kone, A.]] | ||
[[Category: Serre, L.]] | [[Category: Serre, L.]] | ||
| - | [[Category: D12]] | ||
[[Category: detergent]] | [[Category: detergent]] | ||
[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
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[[Category: thiol]] | [[Category: thiol]] | ||
| - | ''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 23:56:19 2008'' |
Revision as of 20:56, 30 March 2008
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| , resolution 2.6Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | DSBA, PPFA, DSF, B3860, Z5392, ECS4783 (Escherichia coli O157:H7) | ||||||
| Related: | 1DSB, 1FVK
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
crystal structure of a mutant DsbA
Overview
Escherichia coli DsbA belongs to the thioredoxin family and catalyzes the formation of disulfide bonds during the folding of proteins in the bacterial periplasm. It active site (C30-P31-H32-C33) consists of a disulfide bridge that is transferred to newly translocated proteins. The work reported here refers to the DsbA mutant termed C33A that retains, towards reduced unfolded thrombin inhibitor, an activity comparable with the wild-type enzyme. Besides, C33A is also able to form a stable covalent complex with DsbB, the membrane protein responsible for maintaining DsbA in its active form. We have determined the crystal structure of C33A at 2.0 angstroms resolution. Although the general architecture of wt DsbA is conserved, we observe the trans/cis isomerization of P31 in the active site and further conformational changes in the so-called "peptide binding groove" region. Interestingly, these modifications involve residues that are specific to DsbA but not to the thioredoxin family fold. The C33A crystal structure exhibits as well a hydrophobic ligand bound close to the active site of the enzyme. The structural analysis of C33A may actually explain the peculiar behavior of this mutant in regards with its interaction with DsbB and thus provides new insights for understanding the catalytic cycle of DsbA.
About this Structure
1TI1 is a Single protein structure of sequence from Escherichia coli o157:h7. Full crystallographic information is available from OCA.
Reference
Intriguing conformation changes associated with the trans/cis isomerization of a prolyl residue in the active site of the DsbA C33A mutant., Ondo-Mbele E, Vives C, Kone A, Serre L, J Mol Biol. 2005 Apr 1;347(3):555-63. PMID:15755450
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