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1typ

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{{STRUCTURE_1typ| PDB=1typ | SCENE= }}
{{STRUCTURE_1typ| PDB=1typ | SCENE= }}
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'''SUBSTRATE INTERACTIONS BETWEEN TRYPANOTHIONE REDUCTASE AND N1-GLUTATHIONYLSPERMIDINE DISULPHIDE AT 0.28-NM RESOLUTION'''
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===SUBSTRATE INTERACTIONS BETWEEN TRYPANOTHIONE REDUCTASE AND N1-GLUTATHIONYLSPERMIDINE DISULPHIDE AT 0.28-NM RESOLUTION===
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==Overview==
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The enzyme trypanothione reductase has been identified as a prime target for the rational design of inhibitors which may have clinical use in the treatment of tropical diseases caused by the genera Trypanosoma and Leishmania. To aid the design or identification of new inhibitors of this enzyme we have elucidated the structural detail of a trypanothione reductase complexed with one of the naturally occurring substrates, N1-glutathionylspermidine disulphide, by single-crystal X-ray diffraction methods at 0.28-nm resolution. The model for the Crithidia fasciculata enzyme-substrate complex has an R-factor of 14.8% and root-mean-square deviations of 0.0015 nm and 3.3 degrees on bond lengths and angles respectively. Hydrogen bonding and van der Waals interactions between the enzyme and substrate are dominated by the amino acid side chains. The substrate binds in a rigid active site such that one glutathione moiety is in a V-shape, the other in an extended conformation. One spermidine moiety binds closely to a hydrophobic patch in the active site formed by a tryptophan and a methionine. Distances between the methionine S delta and the terminal N of this spermidine suggest that a hydrogen bond may supplement the hydrophobic interactions in this part of the active site.
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(as it appears on PubMed at http://www.pubmed.gov), where 8477734 is the PubMed ID number.
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{{ABSTRACT_PUBMED_8477734}}
==About this Structure==
==About this Structure==
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[[Category: Hunter, W N.]]
[[Category: Hunter, W N.]]
[[Category: Oxidoreductase]]
[[Category: Oxidoreductase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 10:31:48 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 20:19:33 2008''

Revision as of 17:19, 28 July 2008

Image:1typ.png

Template:STRUCTURE 1typ

SUBSTRATE INTERACTIONS BETWEEN TRYPANOTHIONE REDUCTASE AND N1-GLUTATHIONYLSPERMIDINE DISULPHIDE AT 0.28-NM RESOLUTION

Template:ABSTRACT PUBMED 8477734

About this Structure

1TYP is a Single protein structure of sequence from Crithidia fasciculata. Full crystallographic information is available from OCA.

Reference

Substrate interactions between trypanothione reductase and N1-glutathionylspermidine disulphide at 0.28-nm resolution., Bailey S, Smith K, Fairlamb AH, Hunter WN, Eur J Biochem. 1993 Apr 1;213(1):67-75. PMID:8477734

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