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[[Image:3tmn.gif|left|200px]]
{{Seed}}
[[Image:3tmn.png|left|200px]]


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{{STRUCTURE_3tmn|  PDB=3tmn  |  SCENE=  }}  
{{STRUCTURE_3tmn|  PDB=3tmn  |  SCENE=  }}  


'''THE BINDING OF L-VALYL-L-TRYPTOPHAN TO CRYSTALLINE THERMOLYSIN ILLUSTRATES THE MODE OF INTERACTION OF A PRODUCT OF PEPTIDE HYDROLYSIS'''
===THE BINDING OF L-VALYL-L-TRYPTOPHAN TO CRYSTALLINE THERMOLYSIN ILLUSTRATES THE MODE OF INTERACTION OF A PRODUCT OF PEPTIDE HYDROLYSIS===




==Overview==
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Crystallographic analysis of the binding of mercaptoacetyl-L-valyl-L-tryptophan to thermolysin suggests that this inhibitor is hydrolyzed by the crystalline enzyme. The apparent product of hydrolysis, L-valyl-L-tryptophan (Val-Trp), occupies the S1'-S2' subsites of the active site, not the S1-S1' subsites as observed previously for the dipeptide L-alanyl-L-phenylalanine (Ala-Phe). The difference in binding of Val-Trp and Ala-Phe is consistent with the specificity requirements and preferences of thermolysin. The binding of Val-Trp illustrates the mode of interaction of one of the products of peptide hydrolysis. High resolution crystallographic refinement indicates that the valyl amino group makes three hydrogen bonds to the enzyme and to solvent and, in addition, is 2.8 A from the carboxylate of Glu-143. This is the first instance in which a direct interaction has been observed between Glu-143 and the scissile nitrogen. As such, the study directly supports the mechanism of action for thermolysin proposed by Hangauer et al. (Hangauer, D. G., Monzingo, A. F., and Matthews, B. W. (1984) Biochemistry 23, 5730-5741) and, by analogy, indirectly supports the similar mechanism proposed for carboxypeptidase A (Monzingo, A. F., and Matthews, B. W. (1984) Biochemistry 23, 5724-5729).
The line below this paragraph, {{ABSTRACT_PUBMED_3343246}}, adds the Publication Abstract to the page
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{{ABSTRACT_PUBMED_3343246}}


==About this Structure==
==About this Structure==
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[[Category: Holden, H M.]]
[[Category: Holden, H M.]]
[[Category: Matthews, B W.]]
[[Category: Matthews, B W.]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Apr 30 13:58:44 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul  3 13:09:46 2008''

Revision as of 10:09, 3 July 2008

File:3tmn.png

Template:STRUCTURE 3tmn

THE BINDING OF L-VALYL-L-TRYPTOPHAN TO CRYSTALLINE THERMOLYSIN ILLUSTRATES THE MODE OF INTERACTION OF A PRODUCT OF PEPTIDE HYDROLYSIS

Template:ABSTRACT PUBMED 3343246

About this Structure

3TMN is a Single protein structure of sequence from Bacillus thermoproteolyticus. Full crystallographic information is available from OCA.

Reference

The binding of L-valyl-L-tryptophan to crystalline thermolysin illustrates the mode of interaction of a product of peptide hydrolysis., Holden HM, Matthews BW, J Biol Chem. 1988 Mar 5;263(7):3256-60. PMID:3343246

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