View source for 3fpe


==Crystal Structure of MtNAS in complex with thermonicotianamine==
<StructureSection load='3fpe' size='340' side='right'caption='[[3fpe]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3fpe]] is a 2 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=3FPE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FPE 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]] 1.7&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BR:BROMIDE+ION'>BR</scene>, <scene name='pdbligand=TNA:N-[(3S)-3-{[(3S)-3-AMINO-3-CARBOXYPROPYL]AMINO}-3-CARBOXYPROPYL]-L-GLUTAMIC+ACID'>TNA</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=3fpe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fpe OCA], [https://pdbe.org/3fpe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3fpe RCSB], [https://www.ebi.ac.uk/pdbsum/3fpe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3fpe ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/O26771_METTH O26771_METTH] 
== 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/fp/3fpe_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=3fpe ConSurf].
<div style="clear:both"></div>
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== Publication Abstract from PubMed ==
Nicotianamine (NA), a small molecule ubiquitous in plants, is an important divalent metal chelator and the main precursor of phytosiderophores. Nicotianamine synthase (NAS) is the enzyme catalyzing NA synthesis by the condensation of three aminopropyl moieties of S-adenosylmethionine (SAM) and the cyclization of one of them to form an azetidine ring. Here we report five crystal structures of an archaeal NAS from Methanothermobacter thermautotrophicus, either free or in complex with its product(s) and substrate(s). These structures reveal a two-domains fold arrangement of MtNAS, a small molecule related to NA (named here thermoNicotianamine or tNA), and an original mechanism of synthesis in a buried reaction chamber. This reaction chamber is open to the solvent through a small inlet, and a single active site allows the selective entrance of only one substrate at a time that is then processed and translocated stepwise.

Crystallographic snapshots of iterative substrate translocations during nicotianamine synthesis in Archaea.,Dreyfus C, Lemaire D, Mari S, Pignol D, Arnoux P Proc Natl Acad Sci U S A. 2009 Sep 22;106(38):16180-4. Epub 2009 Sep 2. PMID:19805277<ref>PMID:19805277</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3fpe" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Methanothermobacter thermautotrophicus str. Delta H]]
[[Category: Arnoux P]]
[[Category: Dreyfus C]]
[[Category: Pignol D]]