3o31: Difference between revisions
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==E81Q mutant of MtNAS in complex with a reaction intermediate== | |||
<StructureSection load='3o31' size='340' side='right' caption='[[3o31]], [[Resolution|resolution]] 1.70Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3o31]] is a 2 chain structure with sequence from [http://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=3O31 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3O31 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=3O3:N-[(3S)-3-AMINO-3-CARBOXYPROPYL]-L-GLUTAMIC+ACID'>3O3</scene>, <scene name='pdbligand=BR:BROMIDE+ION'>BR</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3fpe|3fpe]], [[3fpf|3fpf]], [[3fpg|3fpg]], [[3fph|3fph]], [[3fpj|3fpj]]</td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MTH675, MTH_675 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=187420 Methanothermobacter thermautotrophicus str. Delta H])</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3o31 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o31 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3o31 RCSB], [http://www.ebi.ac.uk/pdbsum/3o31 PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
We determined the three-dimensional structure of a complex between an archaeal nicotianamine synthase homologue and a chemically synthesised reaction intermediate. This structure suggests that the enzymes cavity allows both an ordered substrate binding and provides energetic coupling of the reaction intermediate formation and translocation. | |||
The crystallographic structure of thermoNicotianamine synthase with a synthetic reaction intermediate highlights the sequential processing mechanism.,Dreyfus C, Larrouy M, Cavelier F, Martinez J, Pignol D, Arnoux P Chem Commun (Camb). 2011 May 28;47(20):5825-7. Epub 2011 Apr 12. PMID:21487608<ref>PMID:21487608</ref> | |||
== | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Methanothermobacter thermautotrophicus str. delta h]] | [[Category: Methanothermobacter thermautotrophicus str. delta h]] | ||
[[Category: Arnoux, P.]] | [[Category: Arnoux, P.]] | ||
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[[Category: Pignol, D.]] | [[Category: Pignol, D.]] | ||
[[Category: Biosynthetic protein]] | [[Category: Biosynthetic protein]] | ||
[[Category: | [[Category: Rossmann fold]] | ||
[[Category: Thermonicotianamine synthase]] | [[Category: Thermonicotianamine synthase]] | ||