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1ti1

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[[Image:1ti1.gif|left|200px]]<br /><applet load="1ti1" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1ti1.gif|left|200px]]
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caption="1ti1, resolution 2.6&Aring;" />
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'''crystal structure of a mutant DsbA'''<br />
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{{Structure
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|PDB= 1ti1 |SIZE=350|CAPTION= <scene name='initialview01'>1ti1</scene>, resolution 2.6&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=D12:DODECANE'>D12</scene>
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|ACTIVITY=
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|GENE= DSBA, PPFA, DSF, B3860, Z5392, ECS4783 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=168807 Escherichia coli O127:H6])
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}}
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'''crystal structure of a mutant DsbA'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1TI1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_o127:h6 Escherichia coli o127:h6] with <scene name='pdbligand=D12:'>D12</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TI1 OCA].
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1TI1 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_o127:h6 Escherichia coli o127:h6]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TI1 OCA].
==Reference==
==Reference==
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=15755450 15755450]
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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 o127:h6]]
[[Category: Escherichia coli o127:h6]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: thiol]]
[[Category: thiol]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:13:42 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:18:35 2008''

Revision as of 12:18, 20 March 2008

Image:1ti1.gif


PDB ID 1ti1

Drag the structure with the mouse to rotate
, resolution 2.6Å
Ligands:
Gene: DSBA, PPFA, DSF, B3860, Z5392, ECS4783 (Escherichia coli O127:H6)
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 o127:h6. 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

Page seeded by OCA on Thu Mar 20 14:18:35 2008

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