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.


1vjw

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1vjw.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1vjw.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1vjw| PDB=1vjw | SCENE= }}
{{STRUCTURE_1vjw| PDB=1vjw | SCENE= }}
-
'''STRUCTURE OF OXIDOREDUCTASE (NADP+(A),FERREDOXIN(A))'''
+
===STRUCTURE OF OXIDOREDUCTASE (NADP+(A),FERREDOXIN(A))===
-
==Overview==
+
<!--
-
BACKGROUND: The characterization of the structural features that account for the high thermostability of some proteins is of great scientific and biotechnological interest. Proteins from hyperthermophilic organisms with optimum growth temperatures of 80 degrees C and higher generally show high intrinsic stabilities. The comparison of high resolution X-ray structures of these proteins with their counterparts from mesophilic organisms has therefore helped to identify potentially stabilizing forces in a number of cases. Small monomeric proteins which comprise only a single domain, such as ferredoxins, are especially suitable for such comparisons since the search for determinants of protein stability is considerably simplified. RESULTS: The 1.75 A crystal structure of the extremely thermostable 1[4Fe-4S] ferredoxin from Thermotoga maritima (FdTm) was determined and compared with other monocluster-containing ferredoxins with different degrees of thermostability. CONCLUSIONS: A comparison of the three-dimensional structure of FdTm with that of ferredoxins from mesophilic organisms suggests that the very high thermostability of FdTm is unexpectedly achieved without large changes of the overall protein structure. Instead, an increased number of potentially stabilizing features is observed in FdTm, compared with mesophilic ferredoxins. These include stabilization of alpha helices, replacement of residues in strained conformation by glycines, strong docking of the N-terminal methionine and an overall increase in the number of hydrogen bonds. Most of these features stabilize several secondary structure elements and improve the overall rigidity of the polypeptide backbone. The decreased flexibility will certainly play a relevant role in shielding the iron-sulfur cluster against physiologically high temperatures and further improve the functional integrity of FdTm.
+
The line below this paragraph, {{ABSTRACT_PUBMED_8939753}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 8939753 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_8939753}}
==About this Structure==
==About this Structure==
Line 31: Line 35:
[[Category: Oxidoreductase]]
[[Category: Oxidoreductase]]
[[Category: Thermostable]]
[[Category: Thermostable]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 12:37:02 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 09:29:28 2008''

Revision as of 06:29, 29 July 2008

Image:1vjw.png

Template:STRUCTURE 1vjw

STRUCTURE OF OXIDOREDUCTASE (NADP+(A),FERREDOXIN(A))

Template:ABSTRACT PUBMED 8939753

About this Structure

1VJW is a Single protein structure of sequence from Thermotoga maritima. Full crystallographic information is available from OCA.

Reference

Small structural changes account for the high thermostability of 1[4Fe-4S] ferredoxin from the hyperthermophilic bacterium Thermotoga maritima., Macedo-Ribeiro S, Darimont B, Sterner R, Huber R, Structure. 1996 Nov 15;4(11):1291-301. PMID:8939753

Page seeded by OCA on Tue Jul 29 09:29:28 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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