2qjt
From Proteopedia
(New page: 200px<br /><applet load="2qjt" size="350" color="white" frame="true" align="right" spinBox="true" caption="2qjt, resolution 2.300Å" /> '''Crystal structure o...) |
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- | [[Image:2qjt.jpg|left|200px]] | + | [[Image:2qjt.jpg|left|200px]] |
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- | '''Crystal structure of a bifunctional NMN adenylyltransferase/ADP ribose pyrophosphatase complexed with AMP and MN ion from Francisella tularensis''' | + | {{Structure |
+ | |PDB= 2qjt |SIZE=350|CAPTION= <scene name='initialview01'>2qjt</scene>, resolution 2.300Å | ||
+ | |SITE= <scene name='pdbsite=AC1:Mn+Binding+Site+For+Residue+A+501'>AC1</scene>, <scene name='pdbsite=AC2:Mn+Binding+Site+For+Residue+A+502'>AC2</scene>, <scene name='pdbsite=AC3:Mn+Binding+Site+For+Residue+A+503'>AC3</scene>, <scene name='pdbsite=AC4:Mn+Binding+Site+For+Residue+A+504'>AC4</scene>, <scene name='pdbsite=AC5:Mn+Binding+Site+For+Residue+B+505'>AC5</scene>, <scene name='pdbsite=AC6:Mn+Binding+Site+For+Residue+B+506'>AC6</scene>, <scene name='pdbsite=AC7:Mn+Binding+Site+For+Residue+B+507'>AC7</scene>, <scene name='pdbsite=AC8:Mn+Binding+Site+For+Residue+A+508'>AC8</scene>, <scene name='pdbsite=AC9:Mn+Binding+Site+For+Residue+B+509'>AC9</scene>, <scene name='pdbsite=BC1:Amp+Binding+Site+For+Residue+A+601'>BC1</scene> and <scene name='pdbsite=BC2:Amp+Binding+Site+For+Residue+B+602'>BC2</scene> | ||
+ | |LIGAND= <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene> and <scene name='pdbligand=AMP:ADENOSINE MONOPHOSPHATE'>AMP</scene> | ||
+ | |ACTIVITY= | ||
+ | |GENE= nadM ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=263 Francisella tularensis]) | ||
+ | }} | ||
+ | |||
+ | '''Crystal structure of a bifunctional NMN adenylyltransferase/ADP ribose pyrophosphatase complexed with AMP and MN ion from Francisella tularensis''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 2QJT is a [ | + | 2QJT is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Francisella_tularensis Francisella tularensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QJT OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/18275811 18275811] |
[[Category: Francisella tularensis]] | [[Category: Francisella tularensis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: two individual domain]] | [[Category: two individual domain]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:26:34 2008'' |
Revision as of 16:26, 20 March 2008
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, resolution 2.300Å | |||||||
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Sites: | , , , , , , , , , and | ||||||
Ligands: | and | ||||||
Gene: | nadM (Francisella tularensis) | ||||||
Coordinates: | save as pdb, mmCIF, xml |
Crystal structure of a bifunctional NMN adenylyltransferase/ADP ribose pyrophosphatase complexed with AMP and MN ion from Francisella tularensis
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.
About this Structure
2QJT is a Single protein structure of sequence from Francisella tularensis. 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 Thu Mar 20 18:26:34 2008
Categories: Francisella tularensis | Single protein | Brautigan, C. | Grishin, N V. | Huang, N. | Magni, G. | Osterman, A. | Raffaelli, N. | Sorci, L. | Zhang, H. | Zhang, X. | AMP | MN | Hydrolase | Transferase | Two individual domain