2tir

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2tir.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:2tir.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2tir| PDB=2tir | SCENE= }}
{{STRUCTURE_2tir| PDB=2tir | SCENE= }}
-
'''CRYSTAL STRUCTURE ANALYSIS OF A MUTANT ESCHERICHIA COLI THIOREDOXIN IN WHICH LYSINE 36 IS REPLACED BY GLUTAMIC ACID'''
+
===CRYSTAL STRUCTURE ANALYSIS OF A MUTANT ESCHERICHIA COLI THIOREDOXIN IN WHICH LYSINE 36 IS REPLACED BY GLUTAMIC ACID===
-
==Overview==
+
<!--
-
The structure of a mutant Escherichia coli thioredoxin with a glutamic acid substituted for a conserved lysine at position 36 adjacent to the active site has been solved using molecular replacement and refined at 2.0-A resolution to a crystallographic residual of 19.9%. The mutant was crystallized in an orthorhombic space group with one molecule in the asymmetric unit. The structure of the mutant thioredoxin shows overall good agreement with the wild-type E. coli thioredoxin. The root-mean-square deviations for all C alpha s are 0.45 and 0.79 A between the mutant structure and the two molecules in the asymmetric unit of the wild-type crystals. Structural changes are seen in several residues in the active-site region preceding the disulfide. A reverse turn of residues 29-32 changes the conformation from a type I to a type II turn. This change may be related to the loss of a hydrogen bond from Lys-36 to the main-chain carbonyl of residue 30 due to the mutation. The C alpha atom of Trp-31 has moved 1.9 A and the indole ring no longer makes hydrogen bonds to the carboxyl group of Asp-61 but instead participates in a crystal contact. The structural differences seen in the mutant thioredoxin may be influenced by the crystal packing. The substituted Glu-36 makes extensive crystal contacts. The static fluorescence of this mutant thioredoxin has a different pH dependence than the wild type.
+
The line below this paragraph, {{ABSTRACT_PUBMED_8098620}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 8098620 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_8098620}}
==About this Structure==
==About this Structure==
Line 27: Line 31:
[[Category: Nikkola, M.]]
[[Category: Nikkola, M.]]
[[Category: Electron transport]]
[[Category: Electron transport]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 17:24:13 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 04:36:33 2008''

Revision as of 01:36, 28 July 2008

Template:STRUCTURE 2tir

CRYSTAL STRUCTURE ANALYSIS OF A MUTANT ESCHERICHIA COLI THIOREDOXIN IN WHICH LYSINE 36 IS REPLACED BY GLUTAMIC ACID

Template:ABSTRACT PUBMED 8098620

About this Structure

2TIR is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Crystal structure analysis of a mutant Escherichia coli thioredoxin in which lysine 36 is replaced by glutamic acid., Nikkola M, Gleason FK, Fuchs JA, Eklund H, Biochemistry. 1993 May 18;32(19):5093-8. PMID:8098620

Page seeded by OCA on Mon Jul 28 04:36:33 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools