3o31

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Current revision (08:05, 9 October 2024) (edit) (undo)
 
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== Function ==
== Function ==
[https://www.uniprot.org/uniprot/O26771_METTH O26771_METTH]
[https://www.uniprot.org/uniprot/O26771_METTH O26771_METTH]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3o31" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>

Current revision

E81Q mutant of MtNAS in complex with a reaction intermediate

PDB ID 3o31

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