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1zdp

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{{STRUCTURE_1zdp| PDB=1zdp | SCENE= }}
{{STRUCTURE_1zdp| PDB=1zdp | SCENE= }}
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'''Crystal Structure Analysis of Thermolysin Complexed with the Inhibitor (S)-thiorphan'''
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===Crystal Structure Analysis of Thermolysin Complexed with the Inhibitor (S)-thiorphan===
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==Overview==
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The three-dimensional structures of (S)-thiorphan and (R)-retro-thiorphan bound to thermolysin have been determined crystallographically and refined to residuals of 0.183 and 0.187 at 1.7-A resolution. Thiorphan [N-[(S)-2-(mercaptomethyl)-1-oxo-3-phenylpropyl]glycine] [HSCH2CH(CH2C6H5)CONHC-H2COOH] and retro-thiorphan [[[(R)-1-(mercaptomethyl)-2-phenylethyl] amino]-3-oxopropanoic acid] [HSCH2CH(CH2C6H5)NHCOCH2COOH] are isomeric thiol-containing inhibitors of endopeptidase EC 24-11 (also called "enkephalinase"). The mode of binding of thiorphan to thermolysin is similar to that of (2-benzyl-3-mercaptopropanoyl)-L-alanylglycinamide [Monzingo, A.F., &amp; Matthews, B.W. (1982) Biochemistry 21, 3390-3394] with the inhibitor sulfur atom coordinated to the active site zinc and the peptide portion forming substrate-like interactions with the enzyme. The isomeric inhibitor retro-thiorphan, which differs from thiorphan by the inversion of an amide bond, utilizes very similar interactions with enzyme. Despite the inversion of the -CO-NH- linkage the carbonyl oxygen and amide nitrogen display very similar hydrogen bonding, as anticipated by B.P. Roques et al. [(1983) Proc. Natl. Acad. Sci. U.S.A. 80, 3178-3182]. These results explain why thermolysin and possibly other zinc endopeptidases such as endopeptidase EC 24-11 fail to discriminate between these retro-inverso inhibitors.
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==About this Structure==
==About this Structure==
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[[Category: Thermostable]]
[[Category: Thermostable]]
[[Category: Zinc endopeptidase]]
[[Category: Zinc endopeptidase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 06:00:52 2008''

Revision as of 03:00, 28 July 2008

Image:1zdp.png

Template:STRUCTURE 1zdp

Crystal Structure Analysis of Thermolysin Complexed with the Inhibitor (S)-thiorphan

Template:ABSTRACT PUBMED 2719912

About this Structure

1ZDP is a Single protein structure of sequence from Bacillus thermoproteolyticus. Full crystallographic information is available from OCA.

Reference

Thiorphan and retro-thiorphan display equivalent interactions when bound to crystalline thermolysin., Roderick SL, Fournie-Zaluski MC, Roques BP, Matthews BW, Biochemistry. 1989 Feb 21;28(4):1493-7. PMID:2719912

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