1txx: Difference between revisions

Revision as of 14:26, 27 July 2008

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File:1txx.png

Template:STRUCTURE 1txx

ACTIVE-SITE VARIANT OF E.COLI THIOREDOXINACTIVE-SITE VARIANT OF E.COLI THIOREDOXIN

Template:ABSTRACT PUBMED 10489448

About this StructureAbout this Structure

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

ReferenceReference

The CXXC motif: crystal structure of an active-site variant of Escherichia coli thioredoxin., Schultz LW, Chivers PT, Raines RT, Acta Crystallogr D Biol Crystallogr. 1999 Sep;55(Pt 9):1533-8. PMID:10489448

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-[[Image:1txx.jpg|left|200px]]
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 {{STRUCTURE_1txx|  PDB=1txx  |  SCENE=  }}
-'''ACTIVE-SITE VARIANT OF E.COLI THIOREDOXIN'''
+===ACTIVE-SITE VARIANT OF E.COLI THIOREDOXIN===
-==Overview==
+<!--
-The 2.2 A crystalline structure of an oxidized active-site variant of Escherichia coli thioredoxin (Trx) has been solved. Trx is a 12 kDa enzyme which catalyzes the oxidation of dithiols and the reduction and isomerization of disulfides in other proteins. Its active site contains the common structural motif CXXC. Protein-disulfide isomerase (PDI), a 57 kDa homolog of Trx, contains four Trx-like domains. The three-dimensional structure of PDI is unknown. PDI-deficient Saccharomyces cerevisiae are inviable. An active-site variant of Trx which complements PDI-deficient yeast has the active-site sequence Cys32-Val33-Trp34-Cys35 (CVWC). The reduction potential of oxidized CVWC Trx (E degrees ' = -0.230 V) is altered significantly from that of the wild-type enzyme (E degrees ' = -0.270 V). However, the structure of the oxidized CVWC enzyme is almost identical to that of wild-type Trx. The addition of valine and tryptophan in the active site is likely to increase the reduction potential, largely by decreasing the pK(a) of the Cys32 thiol in the reduced enzyme. Unlike in wild-type Trx, significant protein-protein contacts occur in the crystal. Protein molecules related by a crystallographic twofold axis form a dimer in the crystal. The dimer forms as an extension of the twisted mixed beta-sheet which composes the backbone of each Trx structure.
+The line below this paragraph, {{ABSTRACT_PUBMED_10489448}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10489448 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_10489448}}
 ==About this Structure==
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 [[Category: Oxidoreductase]]
 [[Category: Redox]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 10:30:12 2008''
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