1to2: Difference between revisions
New page: left|200px<br /><applet load="1to2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1to2, resolution 1.30Å" /> '''crystal structure of... |
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[[Image:1to2.jpg|left|200px]]<br /><applet load="1to2" size=" | [[Image:1to2.jpg|left|200px]]<br /><applet load="1to2" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1to2, resolution 1.30Å" /> | caption="1to2, resolution 1.30Å" /> | ||
'''crystal structure of the complex of subtilisin BPN' with chymotrypsin inhibitor 2 M59K, in pH 9 cryosoak'''<br /> | '''crystal structure of the complex of subtilisin BPN' with chymotrypsin inhibitor 2 M59K, in pH 9 cryosoak'''<br /> | ||
==Overview== | ==Overview== | ||
A series of mutants of chymotrypsin inhibitor 2 (CI2), at residues that | 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. | ||
==About this Structure== | ==About this Structure== | ||
1TO2 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bacillus_amyloliquefaciens Bacillus amyloliquefaciens] and [http://en.wikipedia.org/wiki/Hordeum_vulgare_subsp._vulgare Hordeum vulgare subsp. vulgare] with CA, NA, CIT and 15P as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Subtilisin Subtilisin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.62 3.4.21.62] Full crystallographic information is available from [http:// | 1TO2 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bacillus_amyloliquefaciens Bacillus amyloliquefaciens] and [http://en.wikipedia.org/wiki/Hordeum_vulgare_subsp._vulgare Hordeum vulgare subsp. vulgare] with <scene name='pdbligand=CA:'>CA</scene>, <scene name='pdbligand=NA:'>NA</scene>, <scene name='pdbligand=CIT:'>CIT</scene> and <scene name='pdbligand=15P:'>15P</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Subtilisin Subtilisin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.62 3.4.21.62] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TO2 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Subtilisin]] | [[Category: Subtilisin]] | ||
[[Category: Jr., D | [[Category: Jr., D E.Koshland.]] | ||
[[Category: Kwan, G.]] | [[Category: Kwan, G.]] | ||
[[Category: Lu, C | [[Category: Lu, C J.Karen.]] | ||
[[Category: Radisky, E | [[Category: Radisky, E S.]] | ||
[[Category: 15P]] | [[Category: 15P]] | ||
[[Category: CA]] | [[Category: CA]] | ||
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[[Category: serine protease]] | [[Category: serine protease]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:15:35 2008'' | ||
Revision as of 16:15, 21 February 2008
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crystal structure of the complex of subtilisin BPN' with chymotrypsin inhibitor 2 M59K, in pH 9 cryosoak
OverviewOverview
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.
About this StructureAbout this Structure
1TO2 is a Protein complex structure of sequences from Bacillus amyloliquefaciens and Hordeum vulgare subsp. vulgare with , , and as ligands. Active as Subtilisin, with EC number 3.4.21.62 Full crystallographic information is available from OCA.
ReferenceReference
Binding, proteolytic, and crystallographic analyses of mutations at the protease-inhibitor interface of the subtilisin BPN'/chymotrypsin inhibitor 2 complex., Radisky ES, Kwan G, Karen Lu CJ, Koshland DE Jr, Biochemistry. 2004 Nov 2;43(43):13648-56. PMID:15504027
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