2h29

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(New page: 200px<br /><applet load="2h29" size="450" color="white" frame="true" align="right" spinBox="true" caption="2h29, resolution 2.00&Aring;" /> '''Crystal structure of...)
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[[Image:2h29.gif|left|200px]]<br /><applet load="2h29" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="2h29, resolution 2.00&Aring;" />
 
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'''Crystal structure of Nicotinic acid mononucleotide Adenylyltransferase from Staphylococcus aureus: product bound form 1'''<br />
 
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==Overview==
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==Crystal structure of Nicotinic acid mononucleotide Adenylyltransferase from Staphylococcus aureus: product bound form 1==
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Bacterial nicotinic acid mononucleotide adenylyltransferase (NaMNAT; EC, 2.7.7.18) encoded by the nadD gene, is essential for cell survival and is, thus an attractive target for developing new antibacterial agents. The, NaMNAT catalyzes the transfer of an adenylyl group of ATP to nicotinic, acid mononucleotide (NaMN) to form nicotinic acid dinucleotide (NaAD). Two, independently derived, high-resolution structures of Staphylococcus aureus, NaMNAT-NaAD complexes establish the conserved features of the core, dinucleotide-binding fold with other adenylyltransferases from bacteria to, human despite a limited sequence conservation. The crystal structures, reveal that the nicotinate carboxylates of NaAD are recognized by, interaction with the main-chain amides of Thr85 and Tyr117, a positive, helix dipole and two bridged-water molecules. Unlike other bacterial, adenylyltransferases, where a partially conserved histidine residue, interacts with the nicotinate ring, the Leu44 side-chain interacts with, the nicotinate ring by van der Waals contact. Importantly, the S. aureus, NaMNAT represents a distinct adenylyltransferase subfamily identifiable in, part by common features of dimerization and substrate recognition in the, loop connecting beta5 to beta6 (residues 132-146) and the additional beta6, strand. The unique beta6 strand helps orient the residues in the loop, connecting beta5 to beta6 for substrate/product recognition and allows the, beta7 strand structural flexibility to make key dimer interface, interactions. Taken together, these structural results provide a molecular, basis for understanding the coupled activity and recognition specificity, for S. aureus NaMNAT and for rational design of selective inhibitors.
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<StructureSection load='2h29' size='340' side='right'caption='[[2h29]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[2h29]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H29 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2H29 FirstGlance]. <br>
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2H29 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus] with DND as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2H29 OCA].
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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]] 2&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DND:NICOTINIC+ACID+ADENINE+DINUCLEOTIDE'>DND</scene></td></tr>
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==Reference==
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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=2h29 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h29 OCA], [https://pdbe.org/2h29 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2h29 RCSB], [https://www.ebi.ac.uk/pdbsum/2h29 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2h29 ProSAT]</span></td></tr>
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Crystal structure of nicotinic acid mononucleotide adenylyltransferase from Staphyloccocus aureus: structural basis for NaAD interaction in functional dimer., Han S, Forman MD, Loulakis P, Rosner MH, Xie Z, Wang H, Danley DE, Yuan W, Schafer J, Xu Z, J Mol Biol. 2006 Jul 21;360(4):814-25. Epub 2006 Jun 6. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16784754 16784754]
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</table>
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[[Category: Nicotinate-nucleotide adenylyltransferase]]
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== Function ==
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[[Category: Single protein]]
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[https://www.uniprot.org/uniprot/NADD_STAAC NADD_STAAC] Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD) (By similarity).
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== Evolutionary Conservation ==
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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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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/h2/2h29_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=2h29 ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Staphylococcus aureus]]
[[Category: Staphylococcus aureus]]
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[[Category: Han, S.]]
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[[Category: Han S]]
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[[Category: DND]]
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[[Category: nadd]]
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[[Category: namnat]]
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[[Category: nmnat]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 11:30:44 2007''
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Current revision

Crystal structure of Nicotinic acid mononucleotide Adenylyltransferase from Staphylococcus aureus: product bound form 1

PDB ID 2h29

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