1k4m

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[[Image:1k4m.jpg|left|200px]]
 
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{{Structure
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==Crystal structure of E.coli nicotinic acid mononucleotide adenylyltransferase complexed to deamido-NAD==
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|PDB= 1k4m |SIZE=350|CAPTION= <scene name='initialview01'>1k4m</scene>, resolution 1.9&Aring;
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<StructureSection load='1k4m' size='340' side='right'caption='[[1k4m]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>
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<table><tr><td colspan='2'>[[1k4m]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K4M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1K4M FirstGlance]. <br>
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Nicotinate-nucleotide_adenylyltransferase Nicotinate-nucleotide adenylyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.18 2.7.7.18] </span>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
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|GENE= NADD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr>
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|DOMAIN=
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1k4m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k4m OCA], [https://pdbe.org/1k4m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1k4m RCSB], [https://www.ebi.ac.uk/pdbsum/1k4m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1k4m ProSAT]</span></td></tr>
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|RELATEDENTRY=[[1k4k|1k4k]]
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1k4m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k4m OCA], [http://www.ebi.ac.uk/pdbsum/1k4m PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1k4m RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/NADD_ECOLI NADD_ECOLI] Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
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== Evolutionary Conservation ==
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'''Crystal structure of E.coli nicotinic acid mononucleotide adenylyltransferase complexed to deamido-NAD'''
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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==Overview==
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/k4/1k4m_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1k4m ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
Nicotinamide/Nicotinate mononucleotide (NMN/NaMN) adenylyltransferase is an indispensable enzyme in both de novo biosynthesis and salvage of NAD+ and NADP+. In prokaryotes, it is absolutely required for cell survival, thus representing an attractive target for the development of new broad-spectrum antibacteria inhibitors. The crystal structures of E. coli NaMN adenylyltransferase (NMNAT) and its complex with deamido-NAD (NaAD) revealed that ligand binding causes large conformational changes in several loop regions around the active site. The enzyme specifically recognizes the deamidated pyridine nucleotide through interactions between nicotinate carboxylate with several protein main chain amides and a positive helix dipole. Comparison of E. coli NMNAT with those from archaeal organisms revealed extensive differences in the active site architecture, enzyme-ligand interaction mode, and bound dinucleotide conformations. The bacterial NaMN adenylyltransferase structures described here provide a foundation for structure-based design of specific inhibitors that may have therapeutic potential.
Nicotinamide/Nicotinate mononucleotide (NMN/NaMN) adenylyltransferase is an indispensable enzyme in both de novo biosynthesis and salvage of NAD+ and NADP+. In prokaryotes, it is absolutely required for cell survival, thus representing an attractive target for the development of new broad-spectrum antibacteria inhibitors. The crystal structures of E. coli NaMN adenylyltransferase (NMNAT) and its complex with deamido-NAD (NaAD) revealed that ligand binding causes large conformational changes in several loop regions around the active site. The enzyme specifically recognizes the deamidated pyridine nucleotide through interactions between nicotinate carboxylate with several protein main chain amides and a positive helix dipole. Comparison of E. coli NMNAT with those from archaeal organisms revealed extensive differences in the active site architecture, enzyme-ligand interaction mode, and bound dinucleotide conformations. The bacterial NaMN adenylyltransferase structures described here provide a foundation for structure-based design of specific inhibitors that may have therapeutic potential.
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==About this Structure==
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Crystal structures of E. coli nicotinate mononucleotide adenylyltransferase and its complex with deamido-NAD.,Zhang H, Zhou T, Kurnasov O, Cheek S, Grishin NV, Osterman A Structure. 2002 Jan;10(1):69-79. PMID:11796112<ref>PMID:11796112</ref>
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1K4M is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K4M OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Crystal structures of E. coli nicotinate mononucleotide adenylyltransferase and its complex with deamido-NAD., Zhang H, Zhou T, Kurnasov O, Cheek S, Grishin NV, Osterman A, Structure. 2002 Jan;10(1):69-79. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11796112 11796112]
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</div>
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<div class="pdbe-citations 1k4m" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Nicotinate-nucleotide adenylyltransferase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Cheek S]]
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[[Category: Cheek, S.]]
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[[Category: Grishin NV]]
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[[Category: Grishin, N V.]]
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[[Category: Kurnasov O]]
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[[Category: Kurnasov, O.]]
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[[Category: Osterman A]]
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[[Category: Osterman, A.]]
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[[Category: Zhang H]]
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[[Category: Zhang, H.]]
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[[Category: Zhou T]]
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[[Category: Zhou, T.]]
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[[Category: nucleotidyltransferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:43:20 2008''
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Current revision

Crystal structure of E.coli nicotinic acid mononucleotide adenylyltransferase complexed to deamido-NAD

PDB ID 1k4m

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