2r5w
From Proteopedia
(New page: 200px<br /><applet load="2r5w" size="350" color="white" frame="true" align="right" spinBox="true" caption="2r5w, resolution 2.30Å" /> '''Crystal structure of...) |
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| - | [[Image:2r5w.jpg|left|200px]] | + | [[Image:2r5w.jpg|left|200px]] |
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| - | '''Crystal structure of a bifunctional NMN adenylyltransferase/ADP ribose pyrophosphatase from Francisella tularensis''' | + | {{Structure |
| + | |PDB= 2r5w |SIZE=350|CAPTION= <scene name='initialview01'>2r5w</scene>, resolution 2.30Å | ||
| + | |SITE= <scene name='pdbsite=AC1:Mg+Binding+Site+For+Residue+B+348'>AC1</scene>, <scene name='pdbsite=AC2:Mg+Binding+Site+For+Residue+B+349'>AC2</scene>, <scene name='pdbsite=AC3:Mg+Binding+Site+For+Residue+B+350'>AC3</scene>, <scene name='pdbsite=AC4:Cl+Binding+Site+For+Residue+B+351'>AC4</scene>, <scene name='pdbsite=AC5:Cl+Binding+Site+For+Residue+B+352'>AC5</scene>, <scene name='pdbsite=AC6:Mg+Binding+Site+For+Residue+A+348'>AC6</scene>, <scene name='pdbsite=AC7:Mg+Binding+Site+For+Residue+A+349'>AC7</scene>, <scene name='pdbsite=AC8:Mg+Binding+Site+For+Residue+A+350'>AC8</scene> and <scene name='pdbsite=AC9:Cl+Binding+Site+For+Residue+A+351'>AC9</scene> | ||
| + | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=CL:CHLORIDE ION'>CL</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= nadM ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=119856 Francisella tularensis subsp. tularensis]) | ||
| + | }} | ||
| + | |||
| + | '''Crystal structure of a bifunctional NMN adenylyltransferase/ADP ribose pyrophosphatase from Francisella tularensis''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2R5W is a [ | + | 2R5W is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Francisella_tularensis_subsp._tularensis Francisella tularensis subsp. tularensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2R5W 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 subsp. tularensis]] | [[Category: Francisella tularensis subsp. tularensis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: two domain protein]] | [[Category: two domain protein]] | ||
| - | ''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 18:32:55 2008'' |
Revision as of 16:32, 20 March 2008
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| , resolution 2.30Å | |||||||
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| Sites: | , , , , , , , and | ||||||
| Ligands: | and | ||||||
| Gene: | nadM (Francisella tularensis subsp. tularensis) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of a bifunctional NMN adenylyltransferase/ADP ribose pyrophosphatase 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
2R5W is a Single protein structure of sequence from Francisella tularensis subsp. 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
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