1zdp: Difference between revisions
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[[Image:1zdp.gif|left|200px]] | [[Image:1zdp.gif|left|200px]] | ||
'''Crystal Structure Analysis of Thermolysin Complexed with the Inhibitor (S)-thiorphan''' | {{Structure | ||
|PDB= 1zdp |SIZE=350|CAPTION= <scene name='initialview01'>1zdp</scene>, resolution 1.70Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> and <scene name='pdbligand=TIO:(2-MERCAPTOMETHYL-3-PHENYL-PROPIONYL)-GLYCINE'>TIO</scene> | |||
|ACTIVITY= [http://en.wikipedia.org/wiki/Thermolysin Thermolysin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.27 3.4.24.27] | |||
|GENE= | |||
}} | |||
'''Crystal Structure Analysis of Thermolysin Complexed with the Inhibitor (S)-thiorphan''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1ZDP is a [ | 1ZDP is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_thermoproteolyticus Bacillus thermoproteolyticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZDP OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/2719912 2719912] | ||
[[Category: Bacillus thermoproteolyticus]] | [[Category: Bacillus thermoproteolyticus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: enzyme-inhibitor complex; zinc endopeptidase; gamma turn; thermostable]] | [[Category: enzyme-inhibitor complex; zinc endopeptidase; gamma turn; thermostable]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:34:13 2008'' | ||
Revision as of 16:34, 20 March 2008
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| , resolution 1.70Å | |||||||
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| Ligands: | , and | ||||||
| Activity: | Thermolysin, with EC number 3.4.24.27 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure Analysis of Thermolysin Complexed with the Inhibitor (S)-thiorphan
OverviewOverview
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., & 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.
About this StructureAbout this Structure
1ZDP is a Single protein structure of sequence from Bacillus thermoproteolyticus. Full crystallographic information is available from OCA.
ReferenceReference
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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