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.


2qjo

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2qjo.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:2qjo.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2qjo| PDB=2qjo | SCENE= }}
{{STRUCTURE_2qjo| PDB=2qjo | SCENE= }}
-
'''crystal structure of a bifunctional NMN adenylyltransferase/ADP ribose pyrophosphatase (NadM) complexed with ADPRP and NAD from Synechocystis sp.'''
+
===crystal structure of a bifunctional NMN adenylyltransferase/ADP ribose pyrophosphatase (NadM) complexed with ADPRP and NAD from Synechocystis sp.===
-
==Overview==
+
<!--
-
Bacterial NadM-Nudix is a bifunctional enzyme containing a nicotinamide mononucleotide (NMN) adenylyltransferase and an ADP-ribose (ADPR) pyrophosphatase domain. While most members of this enzyme family, such as that from a model cyanobacterium Synechocystis sp., are involved primarily in nicotinamide adenine dinucleotide (NAD) salvage/recycling pathways, its close homolog in a category-A biodefense pathogen, Francisella tularensis, likely plays a central role in a recently discovered novel pathway of NAD de novo synthesis. The crystal structures of NadM-Nudix from both species, including their complexes with various ligands and catalytic metal ions, revealed detailed configurations of the substrate binding and catalytic sites in both domains. The structure of the N-terminal NadM domain may be exploited for designing new antitularemia therapeutics. The ADPR binding site in the C-terminal Nudix domain is substantially different from that of Escherichia coli ADPR pyrophosphatase, and is more similar to human NUDT9. The latter observation provided new insights into the ligand binding mode of ADPR-gated Ca(2+) channel TRPM2.
+
The line below this paragraph, {{ABSTRACT_PUBMED_18275811}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 18275811 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_18275811}}
==About this Structure==
==About this Structure==
Line 34: Line 38:
[[Category: Transferase]]
[[Category: Transferase]]
[[Category: Two individual domain]]
[[Category: Two individual domain]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 15:04:22 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 06:40:18 2008''

Revision as of 03:40, 29 July 2008

Image:2qjo.png

Template:STRUCTURE 2qjo

crystal structure of a bifunctional NMN adenylyltransferase/ADP ribose pyrophosphatase (NadM) complexed with ADPRP and NAD from Synechocystis sp.

Template:ABSTRACT PUBMED 18275811

About this Structure

2QJO is a Single protein structure of sequence from Synechocystis sp.. Full crystallographic information is available from OCA.

Reference

Bifunctional NMN Adenylyltransferase/ADP-Ribose Pyrophosphatase: Structure and Function in Bacterial NAD Metabolism., Huang N, Sorci L, Zhang X, Brautigam CA, Li X, Raffaelli N, Magni G, Grishin NV, Osterman AL, Zhang H, Structure. 2008 Feb;16(2):196-209. PMID:18275811

Page seeded by OCA on Tue Jul 29 06:40:18 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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