2tir: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
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

File:2tir.png

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

Retrieved from "https://proteopedia.org/index.php?title=2tir&oldid=681351"