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1tm1

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Revision as of 16:24, 12 October 2017

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

Structural highlights

1tm1 is a 2 chain structure with sequence from "bacillus_amyloliquifaciens"_(sic)_fukumoto_1943 "bacillus amyloliquifaciens" (sic) fukumoto 1943 and Horvd. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , ,
Gene:	APR ("Bacillus amyloliquifaciens" (sic) Fukumoto 1943)
Activity:	Subtilisin, with EC number 3.4.21.62
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[SUBT_BACAM] Subtilisin is an extracellular alkaline serine protease, it catalyzes the hydrolysis of proteins and peptide amides. Has a high substrate specificity to fibrin.^[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Peng Y, Huang Q, Zhang RH, Zhang YZ. Purification and characterization of a fibrinolytic enzyme produced by Bacillus amyloliquefaciens DC-4 screened from douchi, a traditional Chinese soybean food. Comp Biochem Physiol B Biochem Mol Biol. 2003 Jan;134(1):45-52. PMID:12524032
↑ Radisky ES, Kwan G, Karen Lu CJ, Koshland DE Jr. Binding, proteolytic, and crystallographic analyses of mutations at the protease-inhibitor interface of the subtilisin BPN'/chymotrypsin inhibitor 2 complex. Biochemistry. 2004 Nov 2;43(43):13648-56. PMID:15504027 doi:http://dx.doi.org/10.1021/bi048797k

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1tm1"

@@ Line 1: / Line 1: @@
 ==CRYSTAL STRUCTURE OF THE COMPLEX OF SUBTILISIN BPN' WITH CHYMOTRYPSIN INHIBITOR 2==
 <StructureSection load='1tm1' size='340' side='right' caption='[[1tm1]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">APR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1390 "Bacillus amyloliquifaciens" (sic) Fukumoto 1943])</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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://pdbe.org/1tm1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1tm1 RCSB], [http://www.ebi.ac.uk/pdbsum/1tm1 PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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://pdbe.org/1tm1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1tm1 RCSB], [http://www.ebi.ac.uk/pdbsum/1tm1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1tm1 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 29: / Line 30: @@
 </div>
 <div class="pdbe-citations 1tm1" style="background-color:#fffaf0;"></div>
-==See Also==
-*[[Chymotrypsin Inhibitor|Chymotrypsin Inhibitor]]
-*[[Subtilisin|Subtilisin]]
 == References ==
 <references/>

1tm1

From Proteopedia

Revision as of 16:24, 12 October 2017

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

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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