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.


2qrl

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2qrl.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2qrl.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2qrl| PDB=2qrl | SCENE= }}
{{STRUCTURE_2qrl| PDB=2qrl | SCENE= }}
-
'''Crystal Structure of Oxalylglycine-bound Saccharopine Dehydrogenase (L-Lys Forming) from Saccharomyces cerevisiae'''
+
===Crystal Structure of Oxalylglycine-bound Saccharopine Dehydrogenase (L-Lys Forming) from Saccharomyces cerevisiae===
-
==Overview==
+
<!--
-
Three structures of saccharopine dehydrogenase (l-lysine-forming) (SDH) have been determined in the presence of sulfate, adenosine monophosphate (AMP), and oxalylglycine (OxGly). In the sulfate-bound structure, a sulfate ion binds in a cleft between the two domains of SDH, occupies one of the substrate carboxylate binding sites, and results in partial closure of the active site of the enzyme due to a domain rotation of almost 12 degrees in comparison to the apoenzyme structure. In the second structure, AMP binds to the active site in an area where the NAD+ cofactor is expected to bind. All of the AMP moieties (adenine ring, ribose, and phosphate) interact with specific residues of the enzyme. In the OxGly-bound structure, carboxylates of OxGly interact with arginine residues representative of the manner in which substrate (alpha-ketoglutarate and saccharopine) may bind. The alpha-keto group of OxGly interacts with Lys77 and His96, which are candidates for acid-base catalysis. Analysis of ligand-enzyme interactions, comparative structural analysis, corroboration with kinetic data, and discussion of a ternary complex model are presented in this study.
+
The line below this paragraph, {{ABSTRACT_PUBMED_17939687}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 17939687 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_17939687}}
==About this Structure==
==About this Structure==
Line 35: Line 39:
[[Category: Oxidoreductase]]
[[Category: Oxidoreductase]]
[[Category: Rossmann fold]]
[[Category: Rossmann fold]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 15:32:25 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 14:55:32 2008''

Revision as of 11:55, 28 July 2008

Image:2qrl.png

Template:STRUCTURE 2qrl

Crystal Structure of Oxalylglycine-bound Saccharopine Dehydrogenase (L-Lys Forming) from Saccharomyces cerevisiae

Template:ABSTRACT PUBMED 17939687

About this Structure

2QRL is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

Crystal structures of ligand-bound saccharopine dehydrogenase from Saccharomyces cerevisiae., Andi B, Xu H, Cook PF, West AH, Biochemistry. 2007 Nov 6;46(44):12512-21. Epub 2007 Oct 16. PMID:17939687

Page seeded by OCA on Mon Jul 28 14:55:32 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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