1a2m: Difference between revisions

Revision as of 15:51, 30 June 2008

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File:1a2m.png

Template:STRUCTURE 1a2m

OXIDIZED DSBA AT 2.7 ANGSTROMS RESOLUTION, CRYSTAL FORM IIIOXIDIZED DSBA AT 2.7 ANGSTROMS RESOLUTION, CRYSTAL FORM III

Template:ABSTRACT PUBMED 9655827

About this StructureAbout this Structure

1A2M is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structures of reduced and oxidized DsbA: investigation of domain motion and thiolate stabilization., Guddat LW, Bardwell JC, Martin JL, Structure. 1998 Jun 15;6(6):757-67. PMID:9655827

Page seeded by OCA on Mon Jun 30 15:51:33 2008

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-[[Image:1a2m.gif|left|200px]]
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 {{STRUCTURE_1a2m|  PDB=1a2m  |  SCENE=  }}
-'''OXIDIZED DSBA AT 2.7 ANGSTROMS RESOLUTION, CRYSTAL FORM III'''
+===OXIDIZED DSBA AT 2.7 ANGSTROMS RESOLUTION, CRYSTAL FORM III===
-==Overview==
+<!--
-BACKGROUND: The redox proteins that incorporate a thioredoxin fold have diverse properties and functions. The bacterial protein-folding factor DsbA is the most oxidizing of the thioredoxin family. DsbA catalyzes disulfide-bond formation during the folding of secreted proteins. The extremely oxidizing nature of DsbA has been proposed to result from either domain motion or stabilizing active-site interactions in the reduced form. In the domain motion model, hinge bending between the two domains of DsbA occurs as a result of redox-related conformational changes. RESULTS: We have determined the crystal structures of reduced and oxidized DsbA in the same crystal form and at the same pH (5.6). The crystal structure of a lower pH form of oxidized DsbA has also been determined (pH 5.0). These new crystal structures of DsbA, and the previously determined structure of oxidized DsbA at pH 6.5, provide the foundation for analysis of structural changes that occur upon reduction of the active-site disulfide bond. CONCLUSIONS: The structures of reduced and oxidized DsbA reveal that hinge bending motions do occur between the two domains. These motions are independent of redox state, however, and therefore do not contribute to the energetic differences between the two redox states. Instead, the observed domain motion is proposed to be a consequence of substrate binding. Furthermore, DsbA's highly oxidizing nature is a result of hydrogen bond, electrostatic and helix-dipole interactions that favour the thiolate over the disulfide at the active site.
+The line below this paragraph, {{ABSTRACT_PUBMED_9655827}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 9655827 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_9655827}}
 ==About this Structure==
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 [[Category: Redox protein]]
 [[Category: Redox-active center]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 09:43:04 2008''
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