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.


1v9l

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1v9l.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1v9l.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1v9l| PDB=1v9l | SCENE= }}
{{STRUCTURE_1v9l| PDB=1v9l | SCENE= }}
-
'''L-glutamate dehydrogenase from Pyrobaculum islandicum complexed with NAD'''
+
===L-glutamate dehydrogenase from Pyrobaculum islandicum complexed with NAD===
-
==Overview==
+
<!--
-
The extremely thermostable NAD-dependent glutamate dehydrogenase (NAD-GluDH) from Pyrobaculum islandicum, a member of the Crenarchaeota, was crystallized, and its 3D structure has been determined by X-ray diffraction methods. The homohexameric structure of Pb. islandicum glutamate dehydrogenase (Pis-GluDH) was solved and refined at a resolution of 2.9A with a crystallographic R-factor of 19.9% (Rfree 26.0%). The structure indicates that each subunit consists of two domains separated by a deep cleft containing an active site. The secondary structural elements and catalytically important residues of the enzyme were highly conserved among the NAD(P)-dependent GluDHs from other sources. A structural comparison of Pis-GluDH with other NAD(P)-dependent GluDHs suggests that a significant difference in the alpha8-loop-alpha9 region of this enzyme is associated with its coenzyme specificity. From the analysis of the 3D structure, hydrophobic interactions between intersubunits were found to be important features for the enzyme oligomerization. It has been reported that Pis-GluDH is highly thermostable, like the GluDH of the hyperthermophilic archaeum Pyrococcus furiosus, and the increase in the intersubunit ion pair networks is responsible for the extreme thermostability of the Pc. furiosus enzyme. However, the number of intersubunit ion pairs in the Pis-GluDH molecules is much smaller than those of the Pc. furiosus GluDH. The number of hydrophobic interactions at the intersubunit interfaces were increased and responsible for the extremely high thermostability. This indicates that the major molecular strategy for high thermostability of the GluDHs may be different for each hyperthermophile.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15571725}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15571725 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15571725}}
==About this Structure==
==About this Structure==
Line 20: Line 24:
==Reference==
==Reference==
The first crystal structure of hyperthermostable NAD-dependent glutamate dehydrogenase from Pyrobaculum islandicum., Bhuiya MW, Sakuraba H, Ohshima T, Imagawa T, Katunuma N, Tsuge H, J Mol Biol. 2005 Jan 14;345(2):325-37. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15571725 15571725]
The first crystal structure of hyperthermostable NAD-dependent glutamate dehydrogenase from Pyrobaculum islandicum., Bhuiya MW, Sakuraba H, Ohshima T, Imagawa T, Katunuma N, Tsuge H, J Mol Biol. 2005 Jan 14;345(2):325-37. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15571725 15571725]
 +
 +
Enzymological characteristics of the hyperthermostable NAD-dependent glutamate dehydrogenase from the archaeon Pyrobaculum islandicum and effects of denaturants and organic solvents., Kujo C, Ohshima T, Appl Environ Microbiol. 1998 Jun;64(6):2152-7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9603828 9603828]
[[Category: Glutamate dehydrogenase]]
[[Category: Glutamate dehydrogenase]]
[[Category: Pyrobaculum islandicum]]
[[Category: Pyrobaculum islandicum]]
Line 30: Line 36:
[[Category: Tsuge, H.]]
[[Category: Tsuge, H.]]
[[Category: Protein-nad complex]]
[[Category: Protein-nad complex]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 12:15:59 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 09:33:54 2008''

Revision as of 06:33, 28 July 2008

Image:1v9l.png

Template:STRUCTURE 1v9l

L-glutamate dehydrogenase from Pyrobaculum islandicum complexed with NAD

Template:ABSTRACT PUBMED 15571725

About this Structure

1V9L is a Single protein structure of sequence from Pyrobaculum islandicum. Full crystallographic information is available from OCA.

Reference

The first crystal structure of hyperthermostable NAD-dependent glutamate dehydrogenase from Pyrobaculum islandicum., Bhuiya MW, Sakuraba H, Ohshima T, Imagawa T, Katunuma N, Tsuge H, J Mol Biol. 2005 Jan 14;345(2):325-37. PMID:15571725

Enzymological characteristics of the hyperthermostable NAD-dependent glutamate dehydrogenase from the archaeon Pyrobaculum islandicum and effects of denaturants and organic solvents., Kujo C, Ohshima T, Appl Environ Microbiol. 1998 Jun;64(6):2152-7. PMID:9603828

Page seeded by OCA on Mon Jul 28 09:33:54 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1v9l"
Personal tools