2iv0

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2iv0.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:2iv0.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2iv0| PDB=2iv0 | SCENE= }}
{{STRUCTURE_2iv0| PDB=2iv0 | SCENE= }}
-
'''THERMAL STABILITY OF ISOCITRATE DEHYDROGENASE FROM ARCHAEOGLOBUS FULGIDUS STUDIED BY CRYSTAL STRUCTURE ANALYSIS AND ENGINEERING OF CHIMERS'''
+
===THERMAL STABILITY OF ISOCITRATE DEHYDROGENASE FROM ARCHAEOGLOBUS FULGIDUS STUDIED BY CRYSTAL STRUCTURE ANALYSIS AND ENGINEERING OF CHIMERS===
-
==Overview==
+
<!--
-
Isocitrate dehydrogenase from Archaeoglobus fulgidus (AfIDH) has an apparent melting temperature (T(m)) of 98.5 degrees C. To identify the structural features involved in thermal stabilization of AfIDH, the structure was solved to 2.5 A resolution. AfIDH was strikingly similar to mesophilic IDH from Escherichia coli (EcIDH) and displayed almost the same number of ion pairs and ionic networks. However, two unique inter-domain networks were present in AfIDH; one three-membered ionic network between the large and the small domain and one four-membered ionic network between the clasp and the small domain. The latter ionic network was presumably reduced in size when the clasp domain of AfIDH was swapped with that of EcIDH and the T (m) decreased by 18 degrees C. Contrarily, EcIDH was only stabilized by 4 degrees C by the clasp domain of AfIDH, a result probably due to the introduction of a unique inter-subunit aromatic cluster in AfIDH that may strengthen the dimeric interface in this enzyme. A unique aromatic cluster was identified close to the N-terminus of AfIDH that could provide additional stabilization of this region. Common and unique heat adaptive traits of AfIDH with those recently observed for hyperthermophilic IDH from Aeropyrum pernix (ApIDH) and Thermotoga maritima (TmIDH) are discussed herein.
+
The line below this paragraph, {{ABSTRACT_PUBMED_17401542}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 17401542 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_17401542}}
==About this Structure==
==About this Structure==
Line 40: Line 44:
[[Category: Thermal stability]]
[[Category: Thermal stability]]
[[Category: Tricarboxylic acid cycle]]
[[Category: Tricarboxylic acid cycle]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 07:55:18 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 20:37:03 2008''

Revision as of 17:37, 27 July 2008

Image:2iv0.png

Template:STRUCTURE 2iv0

THERMAL STABILITY OF ISOCITRATE DEHYDROGENASE FROM ARCHAEOGLOBUS FULGIDUS STUDIED BY CRYSTAL STRUCTURE ANALYSIS AND ENGINEERING OF CHIMERS

Template:ABSTRACT PUBMED 17401542

About this Structure

2IV0 is a Single protein structure of sequence from Archaeoglobus fulgidus. Full crystallographic information is available from OCA.

Reference

Thermal stability of isocitrate dehydrogenase from Archaeoglobus fulgidus studied by crystal structure analysis and engineering of chimers., Stokke R, Karlstrom M, Yang N, Leiros I, Ladenstein R, Birkeland NK, Steen IH, Extremophiles. 2007 May;11(3):481-93. Epub 2007 Mar 31. PMID:17401542

Page seeded by OCA on Sun Jul 27 20:37:03 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2iv0"
Personal tools