View source for 4yp6


==Crystal structure of Methanobacterium thermoautotrophicum NMNAT in complex with NADP==
<StructureSection load='4yp6' size='340' side='right'caption='[[4yp6]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4yp6]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanothermobacter_thermautotrophicus_str._Delta_H Methanothermobacter thermautotrophicus str. Delta H]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4YP6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4YP6 FirstGlance]. <br>
</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>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4yp6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4yp6 OCA], [https://pdbe.org/4yp6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4yp6 RCSB], [https://www.ebi.ac.uk/pdbsum/4yp6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4yp6 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/NADM_METTH NADM_METTH] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Nicotinamide mononucleotide adenylyltransferase (NMNAT) catalyzes the biosynthesis of NAD(+) and NaAD(+). The crystal structure of NMNAT from Methanobacterium thermoautotrophicum complexed with NAD(+) and SO4(2-) revealed the active-site residues involved in binding and catalysis. Site-directed mutagenesis was used to further characterize the roles played by several of these residues. Arg11 and Arg136 were implicated in binding the phosphate groups of the ATP substrate. Both of these residues were mutated to lysine individually. Arg47 does not interact with either NMN or ATP substrates directly, but was deemed to play a role in binding as it is proximal to Arg11 and Arg136. Arg47 was mutated to lysine and glutamic acid. Surprisingly, when expressed in Escherichia coli all of these NMNAT mutants trapped a molecule of NADP(+) in their active sites. This NADP(+) was bound in a conformation that was quite different from that displayed by NAD(+) in the native enzyme complex. When NADP(+) was co-crystallized with wild-type NMNAT, the same structural arrangement was observed. These studies revealed a different conformation of NADP(+) in the active site of NMNAT, indicating plasticity of the active site.

Nicotinamide mononucleotide adenylyltransferase displays alternate binding modes for nicotinamide nucleotides.,Pfoh R, Pai EF, Saridakis V Acta Crystallogr D Biol Crystallogr. 2015 Oct;71(Pt 10):2032-9. doi:, 10.1107/S1399004715015497. Epub 2015 Sep 26. PMID:26457427<ref>PMID:26457427</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4yp6" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Methanothermobacter thermautotrophicus str. Delta H]]
[[Category: Christendat D]]
[[Category: Pai EF]]
[[Category: Pfoh R]]
[[Category: Saridakis V]]