1tm3: Difference between revisions

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[[Image:1tm3.~~jpg~~|left|200px]]

[[Image:1tm3.png|left|200px]]

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~~'''~~crystal structure of the complex of subtilisin BPN' with chymotrypsin inhibitor 2 M59k mutant~~'''~~

===crystal structure of the complex of subtilisin BPN' with chymotrypsin inhibitor 2 M59k mutant===

~~==Overview==~~

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~~A series of mutants of chymotrypsin inhibitor 2 (CI2)~~, ~~at residues that interact with~~ the ~~inhibited enzyme subtilisin BPN', were studied~~ to ~~determine~~ the ~~relative importance of intermolecular contacts~~ on ~~either side of the scissile bond~~. ~~Mutants were tested for inhibition of subtilisin, rates of hydrolysis by subtilisin, and ability to acylate subtilisin~~. ~~Additionally~~, ~~crystal structures of~~ the ~~mutant CI2 complexes with subtilisin were obtained~~. Ordered water molecules were found to play an important role in inhibitor recognition, and features of the crystal structures, in combination with biochemical data, support a transition-state stabilization role for the P(1) residue in subtilisin catalysis. Consistent with the proposed mechanism of inhibition, in which rapid acylation is followed by religation, leaving-~~group contacts with the enzyme were found to be more critical determinants of inhibition than acylating~~-~~group contacts in the mutants studied here.~~

The line below this paragraph, {{ABSTRACT_PUBMED_15504027}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 15504027 is the PubMed ID number.

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==About this Structure==

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[[Category: Inhibitor]]

[[Category: Serine protease]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May 3 10~~:07:06 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 20:55:05 2008''

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-[[Image:1tm3.jpg|left|200px]]
+{{Seed}}
+[[Image:1tm3.png|left|200px]]
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 {{STRUCTURE_1tm3|  PDB=1tm3  |  SCENE=  }}
-'''crystal structure of the complex of subtilisin BPN' with chymotrypsin inhibitor 2 M59k mutant'''
+===crystal structure of the complex of subtilisin BPN' with chymotrypsin inhibitor 2 M59k mutant===
-==Overview==
+<!--
-A series of mutants of chymotrypsin inhibitor 2 (CI2), at residues that interact with the inhibited enzyme subtilisin BPN', were studied to determine the relative importance of intermolecular contacts on either side of the scissile bond. Mutants were tested for inhibition of subtilisin, rates of hydrolysis by subtilisin, and ability to acylate subtilisin. Additionally, crystal structures of the mutant CI2 complexes with subtilisin were obtained. Ordered water molecules were found to play an important role in inhibitor recognition, and features of the crystal structures, in combination with biochemical data, support a transition-state stabilization role for the P(1) residue in subtilisin catalysis. Consistent with the proposed mechanism of inhibition, in which rapid acylation is followed by religation, leaving-group contacts with the enzyme were found to be more critical determinants of inhibition than acylating-group contacts in the mutants studied here.
+The line below this paragraph, {{ABSTRACT_PUBMED_15504027}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15504027 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_15504027}}
 ==About this Structure==
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 [[Category: Inhibitor]]
 [[Category: Serine protease]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 10:07:06 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 20:55:05 2008''