1tmn: Difference between revisions

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[[Image:1tmn.jpg|left|200px]]
{{Seed}}
[[Image:1tmn.png|left|200px]]


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{{STRUCTURE_1tmn|  PDB=1tmn  |  SCENE=  }}  
{{STRUCTURE_1tmn|  PDB=1tmn  |  SCENE=  }}  


'''BINDING OF N-CARBOXYMETHYL DIPEPETIDE INHIBITORS TO THERMOLYSIN DETERMINED BY X-RAY CRYSTALLOGRAPHY. A NOVEL CLASS OF TRANSITION-STATE ANALOGUES FOR ZINC PEPTIDASES'''
===BINDING OF N-CARBOXYMETHYL DIPEPETIDE INHIBITORS TO THERMOLYSIN DETERMINED BY X-RAY CRYSTALLOGRAPHY. A NOVEL CLASS OF TRANSITION-STATE ANALOGUES FOR ZINC PEPTIDASES===




==Overview==
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The mode of binding of the specific thermolysin inhibitor N-(1-carboxy-3-phenylpropyl)-L-leucyl-L-tryptophan (KI approximately 5 X 10(-8) M) [Maycock, A. L., DeSousa, D. M., Payne, L. G., ten Broeke, J., Wu, M. T., &amp; Patchett, A. A. (1981) Biochem. Biophys. Res. Commun. 102, 963-969] has been determined by X-ray crystallography and refined to an R value of 17.1% at 1.9-A resolution. The inhibitor binds to thermolysin with both oxygens of the N-carboxymethyl group liganded to the zinc to give overall pentacoordination of the metal. The bidentate ligation of the inhibitor differs from the monodentate binding seen previously for carboxylate-zinc interactions in thermolysin and is closer to the bidentate geometry observed for the binding of hydroxamates [Holmes, M. A., &amp; Matthews, B. W. (1981) Biochemistry 20, 6912-6920]. The geometry of the inhibitor and its interactions with the protein have a number of elements in common with the presumed transition state formed during peptide hydrolysis. The observed zinc ligation supports the previous suggestion that a pentacoordinate intermediate participates in the mechanism of catalysis. However, the alpha-amino nitrogen of the inhibitor is close to Glu-143, suggesting that this residue might accept a proton from an attacking water molecule (as proposed before) and subsequently donate this proton to the leaving nitrogen. By analogy with thermolysin, it is proposed that a related mechanism should be considered for peptide cleavage by carboxypeptidase A.(ABSTRACT TRUNCATED AT 250 WORDS)
The line below this paragraph, {{ABSTRACT_PUBMED_6395881}}, adds the Publication Abstract to the page
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{{ABSTRACT_PUBMED_6395881}}


==About this Structure==
==About this Structure==
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[[Category: Matthews, B W.]]
[[Category: Matthews, B W.]]
[[Category: Monzingo, A F.]]
[[Category: Monzingo, A F.]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 10:08:07 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 03:43:41 2008''

Revision as of 00:43, 29 July 2008

File:1tmn.png

Template:STRUCTURE 1tmn

BINDING OF N-CARBOXYMETHYL DIPEPETIDE INHIBITORS TO THERMOLYSIN DETERMINED BY X-RAY CRYSTALLOGRAPHY. A NOVEL CLASS OF TRANSITION-STATE ANALOGUES FOR ZINC PEPTIDASES

Template:ABSTRACT PUBMED 6395881

About this Structure

1TMN is a Single protein structure. Full crystallographic information is available from OCA.

Reference

Binding of N-carboxymethyl dipeptide inhibitors to thermolysin determined by X-ray crystallography: a novel class of transition-state analogues for zinc peptidases., Monzingo AF, Matthews BW, Biochemistry. 1984 Nov 20;23(24):5724-9. PMID:6395881

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