4xom: Difference between revisions
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<StructureSection load='4xom' size='340' side='right'caption='[[4xom]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='4xom' size='340' side='right'caption='[[4xom]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4xom]] is a 4 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4xom]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_H37Rv Mycobacterium tuberculosis H37Rv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XOM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4XOM FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=4xom FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xom OCA], [https://pdbe.org/4xom PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4xom RCSB], [https://www.ebi.ac.uk/pdbsum/4xom PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4xom ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/FBIB_MYCTU FBIB_MYCTU] Catalyzes the GTP-dependent successive addition of multiple gamma-linked L-glutamates to the L-lactyl phosphodiester of 7,8-didemethyl-8-hydroxy-5-deazariboflavin (F420-0) to form polyglutamated F420 derivatives. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Mycobacterium tuberculosis H37Rv]] | ||
[[Category: Baker | [[Category: Baker EN]] | ||
[[Category: Baker | [[Category: Baker HM]] | ||
[[Category: Bashiri | [[Category: Bashiri G]] | ||
[[Category: Rehan | [[Category: Rehan AM]] | ||
[[Category: Squire | [[Category: Squire CJ]] | ||
Revision as of 20:45, 26 April 2023
Coenzyme F420:L-glutamate ligase (FbiB) from Mycobacterium tuberculosis (C-terminal domain).Coenzyme F420:L-glutamate ligase (FbiB) from Mycobacterium tuberculosis (C-terminal domain).
Structural highlights
FunctionFBIB_MYCTU Catalyzes the GTP-dependent successive addition of multiple gamma-linked L-glutamates to the L-lactyl phosphodiester of 7,8-didemethyl-8-hydroxy-5-deazariboflavin (F420-0) to form polyglutamated F420 derivatives. Publication Abstract from PubMedCofactor F420 is an electron carrier with a major role in the oxidoreductive reactions of Mycobacterium tuberculosis (Mtb), the causative agent of tuberculosis (TB). A gamma-glutamyl ligase catalyzes the final steps of the F420 biosynthesis pathway by successive additions of L-glutamate residues to F420-0, producing a poly-gamma-glutamate tail. The enzyme responsible for this reaction in Archaea (CofE) comprises a single domain and produces F420-2 as the major species. The homologous Mtb enzyme, FbiB, is a two-domain protein and produces F420 with predominantly 5-7 L-glutamate residues in the poly-gamma-glutamate tail. The N-terminal domain of FbiB is homologous to CofE with an annotated gamma-glutamyl ligase activity, whereas the C-terminal domain has sequence similarity to an FMN-dependent family of nitroreductase enzymes. Here we demonstrate that full-length FbiB adds multiple L-glutamate residues to F420-0 in vitro to produce F420-5 after 24 hours; communication between the two domains is critical for full gamma-glutamyl ligase activity. We also present crystal structures of the C-terminal domain of FbiB in apo, F420-0 and FMN bound states, displaying distinct sites for F420-0 and FMN ligands that partially overlap. Finally, we discuss the features of a full-length structural model produced by small angle X-ray scattering (SAXS) and its implications for the role of N- and C-terminal domains in catalysis. Elongation of the poly-gamma-glutamate tail of F420 requires both domains of the F420:gamma-glutamyl ligase (FbiB) of Mycobacterium tuberculosis.,Bashiri G, Rehan AM, Sreebhavan S, Baker HM, Baker EN, Squire CJ J Biol Chem. 2016 Feb 9. pii: jbc.M115.689026. PMID:26861878[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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