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.


1jea

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1jea.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1jea.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1jea| PDB=1jea | SCENE= }}
{{STRUCTURE_1jea| PDB=1jea | SCENE= }}
-
'''ALTERED TOPOLOGY AND FLEXIBILITY IN ENGINEERED SUBTILISIN'''
+
===ALTERED TOPOLOGY AND FLEXIBILITY IN ENGINEERED SUBTILISIN===
-
==Overview==
+
<!--
-
The three-dimensional structures of engineered variants of Bacillus lentus subtilisin having increased enzymatic activity, K27R/N87S/V104Y/N123S/T274A (RSYSA) and N76D/N87S/S103A/V104I (DSAI), were determined by X-ray crystallography. In addition to identifying changes in atomic position we report a method that identifies protein segments having altered flexibility. The method utilizes a statistical analysis of variance to delineate main-chain temperature factors that represent significant departures from the overall variance between equivalent regions seen throughout the structure. This method reveals changes in main-chain mobility in both variants. Residues 125-127 have increased mobility in the RSYSA variant while residues 100-104 have decreased mobility in the DSAI variant. These segments are located at the substrate-binding site and changes in their mobility are believed to relate to the observed changes in proteolytic activity. The effect of altered crystal lattice contacts on segment flexibility becomes apparent when identical variants, determined in two crystal forms, are compared with the native enzyme.
+
The line below this paragraph, {{ABSTRACT_PUBMED_10493860}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 10493860 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_10493860}}
==About this Structure==
==About this Structure==
Line 28: Line 32:
[[Category: Serine protease]]
[[Category: Serine protease]]
[[Category: Sporulation]]
[[Category: Sporulation]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 21:07:03 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 20:06:36 2008''

Revision as of 17:06, 1 July 2008

Image:1jea.png

Template:STRUCTURE 1jea

ALTERED TOPOLOGY AND FLEXIBILITY IN ENGINEERED SUBTILISIN

Template:ABSTRACT PUBMED 10493860

About this Structure

1JEA is a Single protein structure of sequence from Bacillus lentus. Full crystallographic information is available from OCA.

Reference

Engineered Bacillus lentus subtilisins having altered flexibility., Graycar T, Knapp M, Ganshaw G, Dauberman J, Bott R, J Mol Biol. 1999 Sep 10;292(1):97-109. PMID:10493860

Page seeded by OCA on Tue Jul 1 20:06:36 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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