4xgw: Difference between revisions

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'''Unreleased structure'''
==Crystal structure of Escherichia coli Flavin trafficking protein, an FMN transferase, E169K mutant==
<StructureSection load='4xgw' size='340' side='right' caption='[[4xgw]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4xgw]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XGW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4XGW FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4xgv|4xgv]]</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/FAD:protein_FMN_transferase FAD:protein FMN transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.180 2.7.1.180] </span></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=4xgw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xgw OCA], [http://pdbe.org/4xgw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4xgw RCSB], [http://www.ebi.ac.uk/pdbsum/4xgw PDBsum]</span></td></tr>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/APBE_ECOLI APBE_ECOLI]] Involved in the conversion of aminoimidazole ribotide (AIR), a purine intermediate, to the 4-amino-5-hydroxymethyl-2-methyl pyrimidine (HMP) moiety of thiamine (By similarity).
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
We recently reported a flavin-trafficking protein (Ftp) in the syphilis spirochete Treponema pallidum (Ftp_Tp) as the first bacterial metal-dependent FAD pyrophosphatase that hydrolyzes FAD into AMP and FMN in the periplasm. Orthologs of Ftp_Tp in other bacteria (formerly ApbE) appear to lack this hydrolytic activity; rather, they flavinylate the redox subunit, NqrC, via their metal-dependent FMN transferase activity. However, nothing has been known about the nature or mechanism of metal-dependent Ftp catalysis in either Nqr- or Rnf-redox-containing bacteria. In the current study, we identified a bimetal center in the crystal structure of Escherichia coli Ftp (Ftp_Ec) and show via mutagenesis that a single amino acid substitution converts it from an FAD-binding protein to a Mg2+ -dependent FAD pyrophosphatase (Ftp_Tp-like). Furthermore, in the presence of protein substrates, both types of Ftps are capable of flavinylating periplasmic redox-carrying proteins (e.g., RnfG_Ec) via the metal-dependent covalent attachment of FMN. A high-resolution structure of the Ftp-mediated flavinylated protein of Shewanella oneidensis NqrC identified an essential lysine in phosphoester-threonyl-FMN bond formation in the posttranslationally modified flavoproteins. Together, these discoveries broaden our understanding of the physiological capabilities of the bacterial periplasm, and they also clarify a possible mechanism by which flavoproteins are generated.


The entry 4xgw is ON HOLD  until Paper Publication
Molecular insights into the enzymatic diversity of flavin-trafficking protein (Ftp; formerly ApbE) in flavoprotein biogenesis in the bacterial periplasm.,Deka RK, Brautigam CA, Liu WZ, Tomchick DR, Norgard MV Microbiologyopen. 2015 Dec 2. doi: 10.1002/mbo3.306. PMID:26626129<ref>PMID:26626129</ref>


Authors: Tomchick, D.R., Brautigam, C.A., Deka, R.K., Norgard, M.V.
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
Description: Crystal structure of Escherichia coli Flavin trafficking protein, an FMN transferase, E169K mutant
<div class="pdbe-citations 4xgw" style="background-color:#fffaf0;"></div>
[[Category: Unreleased Structures]]
== References ==
[[Category: Norgard, M.V]]
<references/>
[[Category: Tomchick, D.R]]
__TOC__
[[Category: Deka, R.K]]
</StructureSection>
[[Category: Brautigam, C.A]]
[[Category: FAD:protein FMN transferase]]
[[Category: Brautigam, C A]]
[[Category: Deka, R K]]
[[Category: Norgard, M V]]
[[Category: Tomchick, D R]]
[[Category: Bimetal center]]
[[Category: Flavin transferase]]
[[Category: Lipoprotein]]
[[Category: Transferase]]
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