2qjo

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

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-[[Image:2qjo.jpg|left|200px]]
- {{Structure
+==crystal structure of a bifunctional NMN adenylyltransferase/ADP ribose pyrophosphatase (NadM) complexed with ADPRP and NAD from Synechocystis sp.==
-|PDB= 2qjo |SIZE=350|CAPTION= <scene name='initialview01'>2qjo</scene>, resolution 2.60&Aring;
+<StructureSection load='2qjo' size='340' side='right'caption='[[2qjo]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
-|SITE= <scene name='pdbsite=AC1:So4+Binding+Site+For+Residue+A+402'>AC1</scene>, <scene name='pdbsite=AC2:So4+Binding+Site+For+Residue+A+403'>AC2</scene>, <scene name='pdbsite=AC3:So4+Binding+Site+For+Residue+A+404'>AC3</scene>, <scene name='pdbsite=AC4:So4+Binding+Site+For+Residue+B+401'>AC4</scene>, <scene name='pdbsite=AC5:Apr+Binding+Site+For+Residue+A+501'>AC5</scene>, <scene name='pdbsite=AC6:Nad+Binding+Site+For+Residue+A+601'>AC6</scene>, <scene name='pdbsite=AC7:Pop+Binding+Site+For+Residue+A+701'>AC7</scene>, <scene name='pdbsite=AC8:Apr+Binding+Site+For+Residue+B+502'>AC8</scene>, <scene name='pdbsite=AC9:Nad+Binding+Site+For+Residue+B+602'>AC9</scene>, <scene name='pdbsite=BC1:Pop+Binding+Site+For+Residue+B+702'>BC1</scene>, <scene name='pdbsite=BC2:Apr+Binding+Site+For+Residue+C+503'>BC2</scene>, <scene name='pdbsite=BC3:Nad+Binding+Site+For+Residue+C+603'>BC3</scene> and <scene name='pdbsite=BC4:Pop+Binding+Site+For+Residue+C+703'>BC4</scene>
+== Structural highlights ==
-|LIGAND= <scene name='pdbligand=APR:ADENOSINE-5-DIPHOSPHORIBOSE'>APR</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=POP:PYROPHOSPHATE+2-'>POP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
+<table><tr><td colspan='2'>[[2qjo]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Synechocystis_sp._PCC_6803 Synechocystis sp. PCC 6803]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QJO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2QJO FirstGlance]. <br>
-|ACTIVITY=
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
-|GENE= slr0787 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1143 Synechocystis sp.])
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=APR:ADENOSINE-5-DIPHOSPHORIBOSE'>APR</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=POP:PYROPHOSPHATE+2-'>POP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-|DOMAIN=
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2qjo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qjo OCA], [https://pdbe.org/2qjo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2qjo RCSB], [https://www.ebi.ac.uk/pdbsum/2qjo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2qjo ProSAT]</span></td></tr>
-|RELATEDENTRY=
+</table>
-|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2qjo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qjo OCA], [http://www.ebi.ac.uk/pdbsum/2qjo PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2qjo RCSB]</span>
+== Function ==
-}}
+[https://www.uniprot.org/uniprot/NADM_SYNY3 NADM_SYNY3] The Nudix hydrolase domain is active on ADP-ribose, (2')-phospho-ADP-ribose, IDP-ribose and NADPH.
+== Evolutionary Conservation ==
-'''crystal structure of a bifunctional NMN adenylyltransferase/ADP ribose pyrophosphatase (NadM) complexed with ADPRP and NAD from Synechocystis sp.'''
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
-==Overview==
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qj/2qjo_consurf.spt"</scriptWhenChecked>
-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.
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
-==About this Structure==
+  </jmolCheckbox>
-QJO is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Synechocystis_sp. Synechocystis sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QJO OCA].
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2qjo ConSurf].
+<div style="clear:both"></div>
-==Reference==
+__TOC__
-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]
+</StructureSection>
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Synechocystis sp.]]
+[[Category: Synechocystis sp. PCC 6803]]
-[[Category: Brautigan, C.]]
+[[Category: Brautigan C]]
-[[Category: Grishin, N V.]]
+[[Category: Grishin NV]]
-[[Category: Huang, N.]]
+[[Category: Huang N]]
-[[Category: Magni, G.]]
+[[Category: Magni G]]
-[[Category: Osterman, A.]]
+[[Category: Osterman A]]
-[[Category: Raffaelli, N.]]
+[[Category: Raffaelli N]]
-[[Category: Sorci, L.]]
+[[Category: Sorci L]]
-[[Category: Zhang, H.]]
+[[Category: Zhang H]]
-[[Category: Zhang, X.]]
+[[Category: Zhang X]]
-[[Category: hydrolase]]
-[[Category: transferase]]
-[[Category: two individual domain]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:50:00 2008''

2qjo

From Proteopedia

Current revision

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

Structural highlights

Function

Evolutionary Conservation

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