View source for 7mgt


==Ftp from Treponema pallidum bound to an ADP-like inhibitor==
<StructureSection load='7mgt' size='340' side='right'caption='[[7mgt]], [[Resolution|resolution]] 1.54&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7mgt]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Treponema_pallidum Treponema pallidum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7MGT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7MGT 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]] 1.54&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZD4:2-chloroadenosine+5-(trihydrogen+diphosphate)'>ZD4</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=7mgt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7mgt OCA], [https://pdbe.org/7mgt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7mgt RCSB], [https://www.ebi.ac.uk/pdbsum/7mgt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7mgt ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/APBE_TREPA APBE_TREPA] 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 ==
Antibiotic resistance is a challenge for the control of bacterial infections. In an effort to explore unconventional avenues for antibacterial drug development, we focused on the FMN-transferase activity of the enzyme Ftp from the syphilis spirochete, Treponema pallidum (Ftp_Tp). This enzyme, which is only found in prokaryotes and trypanosomatids, post-translationally modifies proteins in the periplasm, covalently linking FMN (from FAD) to proteins that typically are important for establishing an essential electrochemical gradient across the cytoplasmic membrane. As such, Ftp inhibitors potentially represent a new class of antimicrobials. Previously, we showed that AMP is both a product of the Ftp_tp-catalyzed reaction and an inhibitor of the enzyme. As a preliminary step in exploiting this property to develop a novel Ftp_Tp inhibitor, we have used structural and solution studies to examine the inhibitory and enzyme-binding properties of several adenine-based nucleosides, with particular focus on the 2-position of the purine ring. Implications for future drug design are discussed.

Inhibition of bacterial FMN transferase: A potential avenue for countering antimicrobial resistance.,Deka RK, Deka A, Liu WZ, Norgard MV, Brautigam CA Protein Sci. 2021 Nov 19. doi: 10.1002/pro.4241. PMID:34796555<ref>PMID:34796555</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7mgt" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Treponema pallidum]]
[[Category: Brautigam CA]]
[[Category: Deka R]]
[[Category: Norgard MV]]