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.


1vcv

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1vcv.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1vcv.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1vcv| PDB=1vcv | SCENE= }}
{{STRUCTURE_1vcv| PDB=1vcv | SCENE= }}
-
'''Structure of 2-deoxyribose-5-phosphate aldolase from Pyrobaculum aerophilum'''
+
===Structure of 2-deoxyribose-5-phosphate aldolase from Pyrobaculum aerophilum===
-
==Overview==
+
<!--
-
Genes encoding 2-deoxy-d-ribose-5-phosphate aldolase (DERA) homologues from two hyperthermophiles, the archaeon Pyrobaculum aerophilum and the bacterium Thermotoga maritima, were expressed individually in Escherichia coli, after which the structures and activities of the enzymes produced were characterized and compared with those of E. coli DERA. To our surprise, the two hyperthermophilic DERAs showed much greater catalysis of sequential aldol condensation using three acetaldehydes as substrates than the E. coli enzyme, even at a low temperature (25 degrees C), although both enzymes showed much less 2-deoxy-d-ribose-5-phosphate synthetic activity. Both the enzymes were highly resistant to high concentrations of acetaldehyde and retained about 50% of their initial activities after a 20-h exposure to 300 mM acetaldehyde at 25 degrees C, whereas the E. coli DERA was almost completely inactivated after a 2-h exposure under the same conditions. The structure of the P. aerophilum DERA was determined by X-ray crystallography to a resolution of 2.0 A. The main chain coordinate of the P. aerophilum enzyme monomer was quite similar to those of the T. maritima and E. coli enzymes, whose crystal structures have already been solved. However, the quaternary structure of the hyperthermophilic enzymes was totally different from that of the E. coli DERA. The areas of the subunit-subunit interface in the dimer of the hyperthermophilic enzymes are much larger than that of the E. coli enzyme. This promotes the formation of the unique dimeric structure and strengthens the hydrophobic intersubunit interactions. These structural features are considered responsible for the extremely high stability of the hyperthermophilic DERAs.
+
The line below this paragraph, {{ABSTRACT_PUBMED_17905878}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 17905878 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_17905878}}
==About this Structure==
==About this Structure==
Line 33: Line 37:
[[Category: Hyperthermophile]]
[[Category: Hyperthermophile]]
[[Category: Lyase]]
[[Category: Lyase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 12:23:08 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 10:29:41 2008''

Revision as of 07:29, 29 July 2008

Image:1vcv.png

Template:STRUCTURE 1vcv

Structure of 2-deoxyribose-5-phosphate aldolase from Pyrobaculum aerophilum

Template:ABSTRACT PUBMED 17905878

About this Structure

1VCV is a Single protein structure of sequence from Pyrobaculum aerophilum. Full crystallographic information is available from OCA.

Reference

Sequential aldol condensation catalyzed by hyperthermophilic 2-deoxy-d-ribose-5-phosphate aldolase., Sakuraba H, Yoneda K, Yoshihara K, Satoh K, Kawakami R, Uto Y, Tsuge H, Takahashi K, Hori H, Ohshima T, Appl Environ Microbiol. 2007 Nov;73(22):7427-34. Epub 2007 Sep 28. PMID:17905878

Page seeded by OCA on Tue Jul 29 10:29:41 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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