This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1jfu

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1jfu.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1jfu.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1jfu| PDB=1jfu | SCENE= }}
{{STRUCTURE_1jfu| PDB=1jfu | SCENE= }}
-
'''CRYSTAL STRUCTURE OF THE SOLUBLE DOMAIN OF TLPA FROM BRADYRHIZOBIUM JAPONICUM'''
+
===CRYSTAL STRUCTURE OF THE SOLUBLE DOMAIN OF TLPA FROM BRADYRHIZOBIUM JAPONICUM===
-
==Overview==
+
<!--
-
TlpA is an unusual thioredoxin-like protein present in the nitrogen-fixing soil bacterium Bradyrhizobium japonicum. A hydrophobic N-terminal transmembrane domain anchors it to the cytoplasmic membrane, whereby the hydrophilic thioredoxin domain becomes exposed to the periplasmic space. There, TlpA catalyses an essential reaction, probably a reduction, in the biogenesis of cytochrome aa(3). The soluble thioredoxin domain (TlpA(sol)), devoid of the membrane anchor, was purified and crystallized. Oxidized TlpA(sol) crystallized as a non-covalent dimer in the space group P2(1)2(1)2(1). The X-ray structure analysis was carried out by isomorphous replacement using a xenon derivative. This resulted in a high-resolution (1.6 A) three-dimensional structure that displayed all of the features of a classical thioredoxin fold. A number of peculiar structural details were uncovered: (i) Only one of the two active-site-cysteine sulphurs (Cys72, the one closer to the N terminus) is exposed on the surface, making it the likely nucleophile for the reduction of target proteins. (ii) TlpA(sol) possesses a unique structural disulphide bond, formed between Cys10 and Cys155, which connects an unprecedented N-terminal alpha helix with a beta sheet near the C terminus. (iii) An insertion of about 25 amino acid residues, not found in the thioredoxin prototype of Escherichia coli, contributes only marginally to the thioredoxin fold, but forms an extra, surface-exposed alpha helix. This region plus another surface-exposed stretch (-Ile-Gly-Arg-Ala-), which is absent even in the closest TlpA relatives, might be considered as specificity determinants for the recognition of target proteins in the periplasm. The TlpA(sol) structure paves the way towards unraveling important structure-function relationships by rational mutagenesis.
+
The line below this paragraph, {{ABSTRACT_PUBMED_11531338}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 11531338 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_11531338}}
==About this Structure==
==About this Structure==
Line 30: Line 34:
[[Category: Double disulfide bridge]]
[[Category: Double disulfide bridge]]
[[Category: Thioredoxin-like]]
[[Category: Thioredoxin-like]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 21:10:27 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 20:11:09 2008''

Revision as of 17:11, 1 July 2008

Image:1jfu.png

Template:STRUCTURE 1jfu

CRYSTAL STRUCTURE OF THE SOLUBLE DOMAIN OF TLPA FROM BRADYRHIZOBIUM JAPONICUM

Template:ABSTRACT PUBMED 11531338

About this Structure

1JFU is a Single protein structure of sequence from Bradyrhizobium japonicum. Full crystallographic information is available from OCA.

Reference

Structure of the soluble domain of a membrane-anchored thioredoxin-like protein from Bradyrhizobium japonicum reveals unusual properties., Capitani G, Rossmann R, Sargent DF, Grutter MG, Richmond TJ, Hennecke H, J Mol Biol. 2001 Aug 31;311(5):1037-48. PMID:11531338

Page seeded by OCA on Tue Jul 1 20:11:09 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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