This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
3fpe
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 3fpe is ON HOLD until Paper Publication Authors: Dreyfus, C., Pignol, D., Arnoux, P. Description: Crystal Structure of MtNAS in complex with thermo...) |
|||
| (7 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | '''Unreleased structure''' | ||
| - | + | ==Crystal Structure of MtNAS in complex with thermonicotianamine== | |
| + | <StructureSection load='3fpe' size='340' side='right'caption='[[3fpe]], [[Resolution|resolution]] 1.70Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3fpe]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Metth Metth]. 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='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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3fpf|3fpf]], [[3fpg|3fpg]], [[3fph|3fph]], [[3fpj|3fpj]]</div></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MTH675 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=187420 METTH])</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> | ||
| + | == 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/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=3fpe ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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®/PubMed®, 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: Metth]] | ||
| + | [[Category: Arnoux, P]] | ||
| + | [[Category: Dreyfus, C]] | ||
| + | [[Category: Pignol, D]] | ||
| + | [[Category: Biosynthetic protein]] | ||
| + | [[Category: Nicotianamine]] | ||
| + | [[Category: Thermonicotianamine]] | ||
| + | [[Category: Transferase]] | ||
Current revision
Crystal Structure of MtNAS in complex with thermonicotianamine
| |||||||||||
