1tm1

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[[Image:1tm1.jpg|left|200px]]
[[Image:1tm1.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 1tm1 |SIZE=350|CAPTION= <scene name='initialview01'>1tm1</scene>, resolution 1.70&Aring;
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The line below this paragraph, containing "STRUCTURE_1tm1", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE= APR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1390 Bacillus amyloliquefaciens])
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|DOMAIN=
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{{STRUCTURE_1tm1| PDB=1tm1 | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1tm1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tm1 OCA], [http://www.ebi.ac.uk/pdbsum/1tm1 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1tm1 RCSB]</span>
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}}
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'''CRYSTAL STRUCTURE OF THE COMPLEX OF SUBTILISIN BPN' WITH CHYMOTRYPSIN INHIBITOR 2'''
'''CRYSTAL STRUCTURE OF THE COMPLEX OF SUBTILISIN BPN' WITH CHYMOTRYPSIN INHIBITOR 2'''
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[[Category: Lu, C J.Karen.]]
[[Category: Lu, C J.Karen.]]
[[Category: Radisky, E S.]]
[[Category: Radisky, E S.]]
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[[Category: inhibitor]]
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[[Category: Inhibitor]]
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[[Category: serine protease]]
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[[Category: Serine protease]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 10:07:00 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:58:00 2008''
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Revision as of 07:07, 3 May 2008

Image:1tm1.jpg

Template:STRUCTURE 1tm1

CRYSTAL STRUCTURE OF THE COMPLEX OF SUBTILISIN BPN' WITH CHYMOTRYPSIN INHIBITOR 2


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.

About this Structure

1TM1 is a Protein complex structure of sequences from Bacillus amyloliquefaciens and Hordeum vulgare subsp. vulgare. Full crystallographic information is available from OCA.

Reference

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 Page seeded by OCA on Sat May 3 10:07:00 2008

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