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.


1cm7

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1cm7.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1cm7.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1cm7| PDB=1cm7 | SCENE= }}
{{STRUCTURE_1cm7| PDB=1cm7 | SCENE= }}
-
'''3-ISOPROPYLMALATE DEHYDROGENASE FROM ESCHERICHIA COLI'''
+
===3-ISOPROPYLMALATE DEHYDROGENASE FROM ESCHERICHIA COLI===
-
==Overview==
+
<!--
-
The basis of protein stability has been investigated by the structural comparison of themophilic enzymes with their mesophilic counterparts. A number of characteristics have been found that can contribute to the stabilization of thermophilic proteins, but no one is uniquely capable of imparting thermostability. The crystal structure of 3-isopropylmalate dehydrogenase (IPMDH) from the mesophiles Escherichia coli and Salmonella typhimurium have been determined by the method of molecular replacement using the known structure of the homologous Thermus thermophilus enzyme. The structure of the E. coli enzyme was refined at a resolution of 2.1 A to an R-factor of 17.3%, that of the S. typhimurium enzyme at 1.7 A resolution to an R-factor of 19.8%. The three structures were compared to elucidate the basis of the higher thermostability of the T. thermophilus enzyme. A mutant that created a cavity in the hydrophobic core of the thermophilic enzyme was designed to investigate the importance of packing density for thermostability. The structure of this mutant was analyzed. The main stabilizing features in the thermophilic enzyme are an increased number of salt bridges, additional hydrogen bonds, a proportionately larger and more hydrophobic subunit interface, shortened N and C termini and a larger number of proline residues. The mutation in the hydrophobic core of T. thermophilus IPMDH resulted in a cavity of 32 A3, but no significant effect on the activity and thermostability of the mutant was observed.
+
The line below this paragraph, {{ABSTRACT_PUBMED_9086278}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 9086278 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_9086278}}
==About this Structure==
==About this Structure==
Line 32: Line 36:
[[Category: Nad-dependant enzyme]]
[[Category: Nad-dependant enzyme]]
[[Category: Oxidoreductase]]
[[Category: Oxidoreductase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:53:09 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 20:56:23 2008''

Revision as of 17:56, 30 June 2008

Image:1cm7.png

Template:STRUCTURE 1cm7

3-ISOPROPYLMALATE DEHYDROGENASE FROM ESCHERICHIA COLI

Template:ABSTRACT PUBMED 9086278

About this Structure

1CM7 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Crystal structures of Escherichia coli and Salmonella typhimurium 3-isopropylmalate dehydrogenase and comparison with their thermophilic counterpart from Thermus thermophilus., Wallon G, Kryger G, Lovett ST, Oshima T, Ringe D, Petsko GA, J Mol Biol. 1997 Mar 14;266(5):1016-31. PMID:9086278

Page seeded by OCA on Mon Jun 30 20:56:23 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1cm7"
Personal tools