This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1sbn

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1sbn.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1sbn.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1sbn| PDB=1sbn | SCENE= }}
{{STRUCTURE_1sbn| PDB=1sbn | SCENE= }}
-
'''REFINED CRYSTAL STRUCTURES OF SUBTILISIN NOVO IN COMPLEX WITH WILD-TYPE AND TWO MUTANT EGLINS. COMPARISON WITH OTHER SERINE PROTEINASE INHIBITOR COMPLEXES'''
+
===REFINED CRYSTAL STRUCTURES OF SUBTILISIN NOVO IN COMPLEX WITH WILD-TYPE AND TWO MUTANT EGLINS. COMPARISON WITH OTHER SERINE PROTEINASE INHIBITOR COMPLEXES===
-
==Overview==
+
<!--
-
The crystal structures of the complexes formed between subtilisin Novo and three inhibitors, eglin c, Arg45-eglin c and Lys53-eglin c have been determined using molecular replacement and difference Fourier techniques and refined at 2.4 A, 2.1 A, and 2.4 A resolution, respectively. The mutants Arg45-eglin c and Lys53-eglin c were constructed by site-directed mutagenesis in order to investigate the inhibitory specificity and stability of eglin c. Arg45-eglin became a potent trypsin inhibitor, in contrast to native eglin, which is an elastase inhibitor. This specificity change was rationalized by comparing the structures of Arg45-eglin and basic pancreatic trypsin inhibitor and their interactions with trypsin. The residue Arg53, which participates in a complex network of hydrogen bonds formed between the core and the binding loop of eglin c, was replaced with the shorter basic amino acid lysine in the mutant Lys53-eglin. Two hydrogen bonds with Thr44, located in the binding loop, can no longer be formed but are partially restored by a water molecule bound in the vicinity of Lys53. Eglin c in complexes with both subtilisin Novo and subtilisin Carlsberg was crystallized in two different space groups. Comparison of the complexes showed a rigid body rotation for the eglin c core of 11.5 degrees with respect to the enzyme, probably caused by different intermolecular contacts in both crystal forms.
+
The line below this paragraph, {{ABSTRACT_PUBMED_1992167}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 1992167 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_1992167}}
==About this Structure==
==About this Structure==
Line 27: Line 31:
[[Category: Heinz, D W.]]
[[Category: Heinz, D W.]]
[[Category: Priestle, J P.]]
[[Category: Priestle, J P.]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 08:31:01 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 22:01:03 2008''

Revision as of 19:01, 27 July 2008

Image:1sbn.png

Template:STRUCTURE 1sbn

REFINED CRYSTAL STRUCTURES OF SUBTILISIN NOVO IN COMPLEX WITH WILD-TYPE AND TWO MUTANT EGLINS. COMPARISON WITH OTHER SERINE PROTEINASE INHIBITOR COMPLEXES

Template:ABSTRACT PUBMED 1992167

About this Structure

1SBN is a Protein complex structure of sequences from Bacillus subtilis and Hirudo medicinalis. Full crystallographic information is available from OCA.

Reference

Refined crystal structures of subtilisin novo in complex with wild-type and two mutant eglins. Comparison with other serine proteinase inhibitor complexes., Heinz DW, Priestle JP, Rahuel J, Wilson KS, Grutter MG, J Mol Biol. 1991 Jan 20;217(2):353-71. PMID:1992167

Page seeded by OCA on Sun Jul 27 22:01:03 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1sbn"
Personal tools