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New page: left|200px<br /> <applet load="1gzu" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gzu, resolution 2.90Å" /> '''CRYSTAL STRUCTURE O...
 
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[[Image:1gzu.gif|left|200px]]<br />
<applet load="1gzu" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1gzu, resolution 2.90&Aring;" />
'''CRYSTAL STRUCTURE OF HUMAN NICOTINAMIDE MONONUCLEOTIDE ADENYLYLTRANSFERASE IN COMPLEX WITH NMN'''<br />


==Overview==
==Crystal Structure of Human Nicotinamide Mononucleotide Adenylyltransferase in Complex with NMN==
The final step in the biosynthesis of nicotinamide-adenine dinucleotide, a, major coenzyme in cellular redox reactions and involved in intracellular, signaling, is catalyzed by the enzyme nicotinamide mononucleotide, adenylyltransferase (NMNAT). The X-ray structure of human NMNAT in complex, with nicotinamide mononucleotide was solved by the single-wavelength, anomalous dispersion method at a resolution of 2.9 A. Human NMNAT is a, symmetric hexamer whose subunit is formed by a large six-stranded parallel, beta-sheet with helices on both sides. Human NMNAT displays a different, oligomerization compared to the archaeal enzyme. The protein-nicotinamide, mononucleotide interaction pattern provides insight into ligand binding in, the human enzyme.
<StructureSection load='1gzu' size='340' side='right'caption='[[1gzu]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<table><tr><td colspan='2'>[[1gzu]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1gry 1gry]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GZU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GZU FirstGlance]. <br>
1GZU is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]] with NMN as [[http://en.wikipedia.org/wiki/ligand ligand]]. This structure superseeds the now removed PDB entry 1GRY. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.1 2.7.7.1]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GZU OCA]].  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9&#8491;</td></tr>
 
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=NMN:BETA-NICOTINAMIDE+RIBOSE+MONOPHOSPHATE'>NMN</scene></td></tr>
==Reference==
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1gzu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gzu OCA], [https://pdbe.org/1gzu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gzu RCSB], [https://www.ebi.ac.uk/pdbsum/1gzu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gzu ProSAT]</span></td></tr>
Crystal structure of human nicotinamide mononucleotide adenylyltransferase in complex with NMN., Werner E, Ziegler M, Lerner F, Schweiger M, Heinemann U, FEBS Lett. 2002 Apr 10;516(1-3):239-44. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11959140 11959140]
</table>
== Disease ==
[https://www.uniprot.org/uniprot/NMNA1_HUMAN NMNA1_HUMAN] Defects in NMNAT1 are the cause of Leber congenital amaurosis 9 (LCA9) [MIM:[https://omim.org/entry/608553 608553]. A severe dystrophy of the retina, typically becoming evident in the first years of life. Visual function is usually poor and often accompanied by nystagmus, sluggish or near-absent pupillary responses, photophobia, high hyperopia and keratoconus.<ref>PMID:22842230</ref> <ref>PMID:22842231</ref> <ref>PMID:22842229</ref> <ref>PMID:22842227</ref>
== Function ==
[https://www.uniprot.org/uniprot/NMNA1_HUMAN NMNA1_HUMAN] Catalyzes the formation of NAD(+) from nicotinamide mononucleotide (NMN) and ATP. Can also use the deamidated form; nicotinic acid mononucleotide (NaMN) as substrate with the same efficiency. Can use triazofurin monophosphate (TrMP) as substrate. Also catalyzes the reverse reaction, i.e. the pyrophosphorolytic cleavage of NAD(+). For the pyrophosphorolytic activity, prefers NAD(+) and NAAD as substrates and degrades NADH, nicotinic acid adenine dinucleotide phosphate (NHD) and nicotinamide guanine dinucleotide (NGD) less effectively. Fails to cleave phosphorylated dinucleotides NADP(+), NADPH and NAADP(+). Protects against axonal degeneration following mechanical or toxic insults.<ref>PMID:17402747</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gz/1gzu_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1gzu ConSurf].
<div style="clear:both"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Heinemann, U.]]
[[Category: Heinemann U]]
[[Category: Lerner, F.]]
[[Category: Lerner F]]
[[Category: Schweiger, M.]]
[[Category: Schweiger M]]
[[Category: Werner, E.]]
[[Category: Werner E]]
[[Category: Ziegler, M.]]
[[Category: Ziegler M]]
[[Category: NMN]]
[[Category: adenylyltransferase]]
[[Category: nad biosynthesis]]
 
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Retrieved from "https://proteopedia.org/1gzu"