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.


2gru

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2gru.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:2gru.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2gru| PDB=2gru | SCENE= }}
{{STRUCTURE_2gru| PDB=2gru | SCENE= }}
-
'''Crystal structure of 2-deoxy-scyllo-inosose synthase complexed with carbaglucose-6-phosphate, NAD+ and Co2+'''
+
===Crystal structure of 2-deoxy-scyllo-inosose synthase complexed with carbaglucose-6-phosphate, NAD+ and Co2+===
-
==Overview==
+
<!--
-
A key enzyme in the biosynthesis of clinically important aminoglycoside antibiotics is 2-deoxy-scyllo-inosose synthase (DOIS), which catalyzes carbocycle formation from D-glucose-6-phosphate to 2-deoxy-scyllo-inosose through a multistep reaction. This reaction mechanism is similar to the catalysis by dehydroquinate synthase (DHQS) of the cyclization of 3-deoxy-D-arabino-heputulosonate-7-phosphate to dehydroquinate in the shikimate pathway, but significant dissimilarity between these enzymes is also known, particularly in the stereochemistry of the phosphate elimination reaction and the cyclization. Here, the crystal structures of DOIS from Bacillus circulans and its complex with the substrate analog inhibitor carbaglucose-6-phosphate, NAD+, and Co2+ have been determined to provide structural insights into the reaction mechanism. The complex structure shows that an active site exists between the N-terminal and C-terminal domains and that the inhibitor coordinates a cobalt ion in this site. Two subunits exist as a dimer in the asymmetric unit. The two active sites of the dimer were observed to be different. One contains a dephosphorylated compound derived from the inhibitor and the other includes the inhibitor without change. The present study suggested that phosphate elimination proceeds through syn-elimination assisted by Glu 243 and the aldol condensation proceeds via a boat conformation. Also discussed are significant similarities and dissimilarities between DOIS and DHQS, particularly in terms of the structure at the active site and the reaction mechanism.
+
The line below this paragraph, {{ABSTRACT_PUBMED_17879343}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 17879343 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_17879343}}
==About this Structure==
==About this Structure==
Line 28: Line 32:
[[Category: Dehydroquinate synthase]]
[[Category: Dehydroquinate synthase]]
[[Category: Lyase]]
[[Category: Lyase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Apr 30 13:25:35 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 12:25:29 2008''

Revision as of 09:25, 28 July 2008

Image:2gru.png

Template:STRUCTURE 2gru

Crystal structure of 2-deoxy-scyllo-inosose synthase complexed with carbaglucose-6-phosphate, NAD+ and Co2+

Template:ABSTRACT PUBMED 17879343

About this Structure

2GRU is a Single protein structure of sequence from Bacillus circulans. Full crystallographic information is available from OCA.

Reference

Structure of 2-deoxy-scyllo-inosose synthase, a key enzyme in the biosynthesis of 2-deoxystreptamine-containing aminoglycoside antibiotics, in complex with a mechanism-based inhibitor and NAD+., Nango E, Kumasaka T, Hirayama T, Tanaka N, Eguchi T, Proteins. 2008 Feb 1;70(2):517-27. PMID:17879343

Page seeded by OCA on Mon Jul 28 12:25:29 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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