Eur J Biochem. 1991 May 23;198(1):53-7.

Anion binding at the active site of trypanosomal triosephosphate isomerase. Monohydrogen phosphate does not mimic sulphate.

Verlinde CL, Noble ME, Kalk KH, Groendijk H, Wierenga RK, Hol WG.

Source

BIOSON Research Institute, University of Groningen, The Netherlands.

Abstract

The three-dimensional structure of triosephosphate isomerase complexed with the competitive inhibitor SO-4(2) was determined by X-ray crystallography to a resolution of 0.24 nm. A comparison with the native crystal structure, where SO-4(2) is bound, revealed five changes: (a) a 0.10-nm shift of the anion-binding site; (b) a further closing of the flexible loop of the enzyme; (c) a 'swinging in' of the side chain of the catalytic Glu, that is chi 1 changes from (+) to (-) synclinal; (d) an altered water structure; (e) a disappearance of the conformational heterogeneity at the C-terminus of strand beta 7. Some of these changes may be related to the different hydrogen-bond pattern about the two different anions. However, the distance of 0.10 nm between the sulphur and phosphorus positions is unexpected and remains intriguing.

PMID:: 2040290; [PubMed - indexed for MEDLINE]

Free full text

Publication Types, MeSH Terms, Substances

Publication Types

Research Support, Non-U.S. Gov't

MeSH Terms

Substances

LinkOut - more resources

Full Text Sources

Other Literature Sources

COS Scholar Universe

Supplemental Content

Save items

Related citations in PubMed

Structure of the complex between trypanosomal triosephosphate isomerase and N-hydroxy-4-phosphono-butanamide: binding at the active site despite an "open" flexible loop conformation. [Protein Sci. 1992]
Structure of the complex between trypanosomal triosephosphate isomerase and N-hydroxy-4-phosphono-butanamide: binding at the active site despite an "open" flexible loop conformation.
Verlinde CL, Witmans CJ, Pijning T, Kalk KH, Hol WG, Callens M, Opperdoes FR. Protein Sci. 1992 Dec; 1(12):1578-84.
Refined 1.83 A structure of trypanosomal triosephosphate isomerase crystallized in the presence of 2.4 M-ammonium sulphate. A comparison with the structure of the trypanosomal triosephosphate isomerase-glycerol-3-phosphate complex. [J Mol Biol. 1991]
Refined 1.83 A structure of trypanosomal triosephosphate isomerase crystallized in the presence of 2.4 M-ammonium sulphate. A comparison with the structure of the trypanosomal triosephosphate isomerase-glycerol-3-phosphate complex.
Wierenga RK, Noble ME, Vriend G, Nauche S, Hol WG. J Mol Biol. 1991 Aug 20; 220(4):995-1015.
The adaptability of the active site of trypanosomal triosephosphate isomerase as observed in the crystal structures of three different complexes. [Proteins. 1991]
The adaptability of the active site of trypanosomal triosephosphate isomerase as observed in the crystal structures of three different complexes.
Noble ME, Wierenga RK, Lambeir AM, Opperdoes FR, Thunnissen AM, Kalk KH, Groendijk H, Hol WG. Proteins. 1991; 10(1):50-69.
Review On the three-dimensional structure and catalytic mechanism of triose phosphate isomerase. [Philos Trans R Soc Lond B Biol...]
Review On the three-dimensional structure and catalytic mechanism of triose phosphate isomerase.
Alber T, Banner DW, Bloomer AC, Petsko GA, Phillips D, Rivers PS, Wilson IA. Philos Trans R Soc Lond B Biol Sci. 1981 Jun 26; 293(1063):159-71.
Review Crystallographic binding studies with triosephosphate isomerases: conformational changes induced by substrate and substrate-analogues. [FEBS Lett. 1992]
Review Crystallographic binding studies with triosephosphate isomerases: conformational changes induced by substrate and substrate-analogues.
Wierenga RK, Borchert TV, Noble ME. FEBS Lett. 1992 Jul 27; 307(1):34-9.

See reviews... See all...

Cited by 4 PubMed Central articles

Dimeric quaternary structure of the prototypical dual specificity phosphatase VH1. [J Biol Chem. 2009]
Dimeric quaternary structure of the prototypical dual specificity phosphatase VH1.
Koksal AC, Nardozzi JD, Cingolani G. J Biol Chem. 2009 Apr 10; 284(15):10129-37. Epub 2009 Feb 10.
Enzymatic catalysis of proton transfer at carbon: activation of triosephosphate isomerase by phosphite dianion. [Biochemistry. 2007]
Enzymatic catalysis of proton transfer at carbon: activation of triosephosphate isomerase by phosphite dianion.
Amyes TL, Richard JP. Biochemistry. 2007 May 15; 46(19):5841-54. Epub 2007 Apr 20.
Review Protein crystallography and infectious diseases. [Protein Sci. 1994]
Review Protein crystallography and infectious diseases.
Verlinde CL, Merritt EA, Van den Akker F, Kim H, Feil I, Delboni LF, Mande SC, Sarfaty S, Petra PH, Hol WG. Protein Sci. 1994 Oct; 3(10):1670-86.

See all...

Structures reported by this article

Monohydrogen Phosphate Binding To Trypanosomal Triosephosphate Isomerase

PDB: 1AG1

Source: Trypanosoma brucei

Method: X-Ray Diffraction

Resolution: 2.36 Å

Related information

Related Citations
Calculated set of PubMed citations closely related to the selected article(s) retrieved using a word weight algorithm. Related articles are displayed in ranked order from most to least relevant, with the “linked from” citation displayed first.
Substance (MeSH Keyword)
PubChem chemical substance (submitted) records that are classified under the same Medical Subject Headings (MeSH) controlled vocabulary as the current articles.
Taxonomy via GenBank
Taxonomy records associated with the current articles through taxonomic information on related molecular database records (Nucleotide, Protein, Gene, SNP, Structure).
Protein
Protein translation features of primary database (GenBank) nucleotide records reported in the current articles as well as Reference Sequences (RefSeqs) that include the articles as references.
Structure
Three-dimensional structure records in the NCBI Structure database for data reported in the current articles.
Cited in PMC
Full-text articles in the PubMed Central Database that cite the current articles.

Recent activity

Clear Turn Off Turn On

Anion binding at the active site of trypanosomal triosephosphate isomerase. Mono...
Anion binding at the active site of trypanosomal triosephosphate isomerase. Monohydrogen phosphate does not mimic sulphate.
Eur J Biochem. 1991 May 23 ;198(1):53-7.

PubMed
Simple monitoring of cuff tracheal pressures.
Simple monitoring of cuff tracheal pressures.
Anaesthesia. 2010 Feb ;65(2):215.

PubMed
Calcium-dependent binding of basement membrane protein BM-40 (osteonectin, SPARC...
Calcium-dependent binding of basement membrane protein BM-40 (osteonectin, SPARC) to basement membrane collagen type IV.
Eur J Biochem. 1991 May 23 ;198(1):141-50.

PubMed
Social consequences of multiple sclerosis: clinical and demographic predictors -...
Social consequences of multiple sclerosis: clinical and demographic predictors - a historical prospective cohort study.
Eur J Neurol. 2010 Nov ;17(11):1346-51. doi: 10.1111/j.1468-1331.2010.03020.x.

PubMed
Enhanced working and verbal memory after lamotrigine treatment in pediatric bipo...
Enhanced working and verbal memory after lamotrigine treatment in pediatric bipolar disorder.
Bipolar Disord. 2010 Mar ;12(2):213-20.

PubMed

Your browsing activity is empty.

Activity recording is turned off.

Turn recording back on

PubMed

Result Filters

Display Settings:

Send to: