4xoo: Difference between revisions
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==FMN complex of coenzyme F420:L-glutamate ligase (FbiB) from Mycobacterium tuberculosis (C-terminal domain)== | |||
<StructureSection load='4xoo' size='340' side='right'caption='[[4xoo]], [[Resolution|resolution]] 2.10Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4xoo]] 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=4XOO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4XOO 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]] 2.1Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</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=4xoo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xoo OCA], [https://pdbe.org/4xoo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4xoo RCSB], [https://www.ebi.ac.uk/pdbsum/4xoo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4xoo ProSAT]</span></td></tr> | |||
</table> | |||
== 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;"> | |||
== Publication Abstract from PubMed == | |||
Cofactor 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<ref>PMID:26861878</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Baker | <div class="pdbe-citations 4xoo" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
[[Category: Bashiri | <references/> | ||
[[Category: | __TOC__ | ||
[[Category: Squire | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Mycobacterium tuberculosis H37Rv]] | |||
[[Category: Baker EN]] | |||
[[Category: Baker HM]] | |||
[[Category: Bashiri G]] | |||
[[Category: Rehan AM]] | |||
[[Category: Squire CJ]] | |||
Latest revision as of 10:47, 27 September 2023
FMN complex of coenzyme F420:L-glutamate ligase (FbiB) from Mycobacterium tuberculosis (C-terminal domain)FMN complex of 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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