1un2

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1un2.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1un2.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1un2| PDB=1un2 | SCENE= }}
{{STRUCTURE_1un2| PDB=1un2 | SCENE= }}
-
'''CRYSTAL STRUCTURE OF CIRCULARLY PERMUTED CPDSBA_Q100T99 PRESERVED GLOBAL FOLD AND LOCAL STRUCTURAL ADJUSTMENTS'''
+
===CRYSTAL STRUCTURE OF CIRCULARLY PERMUTED CPDSBA_Q100T99 PRESERVED GLOBAL FOLD AND LOCAL STRUCTURAL ADJUSTMENTS===
-
==Overview==
+
<!--
-
The thiol-disulfide oxidoreductase DsbA is required for efficient formation of disulfide bonds in the Escherichia coli periplasm. The enzyme is the strongest oxidant of the family of thioredoxin-like proteins and three-dimensional structures of both oxidized and reduced forms are known. DsbA consists of a catalytic thioredoxin-like domain and a helical domain that is inserted into the thioredoxin motif. Here, the X-ray structure of a circularly permuted variant, cpDsbA(Q100T99), is reported in which the natural termini are joined by the pentapeptide linker GGGTG, leading to a continuous thioredoxin domain, and new termini that have been introduced in the helical domain by breaking the peptide bond Thr99-Gln100. cpDsbA(Q100T99) is catalytically active in vivo and in vitro. The crystal structure of oxidized cpDsbA(Q100T99), determined by molecular replacement at 2.4 A resolution, was found to be very similar to that of wild-type DsbA. The lower thermodynamic stability of cpDsbA(Q100T99) relative to DsbA is associated with small structural changes within the molecule, especially near the new termini and the circularizing linker. The active-site helices and adjacent loops display increased flexibility compared with oxidized DsbA.
+
The line below this paragraph, {{ABSTRACT_PUBMED_14747707}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 14747707 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_14747707}}
==About this Structure==
==About this Structure==
Line 34: Line 38:
[[Category: Redox protein]]
[[Category: Redox protein]]
[[Category: Thioredoxin]]
[[Category: Thioredoxin]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 11:27:02 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 6 00:57:28 2008''

Revision as of 21:57, 5 July 2008

Image:1un2.png

Template:STRUCTURE 1un2

CRYSTAL STRUCTURE OF CIRCULARLY PERMUTED CPDSBA_Q100T99 PRESERVED GLOBAL FOLD AND LOCAL STRUCTURAL ADJUSTMENTS

Template:ABSTRACT PUBMED 14747707

About this Structure

1UN2 is a Single protein structure of sequence from Escherichia coli. This structure supersedes the now removed PDB entry 1dyv. Full crystallographic information is available from OCA.

Reference

Structure of circularly permuted DsbA(Q100T99): preserved global fold and local structural adjustments., Manjasetty BA, Hennecke J, Glockshuber R, Heinemann U, Acta Crystallogr D Biol Crystallogr. 2004 Feb;60(Pt 2):304-9. Epub 2004, Jan 23. PMID:14747707

Page seeded by OCA on Sun Jul 6 00:57:28 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1un2"
Personal tools