View source for 6nsi


==Crystal structure of Fe(III)-bound YtgA from Chlamydia trachomatis==
<StructureSection load='6nsi' size='340' side='right'caption='[[6nsi]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6nsi]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Chlamydia_trachomatis Chlamydia trachomatis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6NSI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6NSI 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]] 2.0000634&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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=6nsi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6nsi OCA], [https://pdbe.org/6nsi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6nsi RCSB], [https://www.ebi.ac.uk/pdbsum/6nsi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6nsi ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Y067_CHLTR Y067_CHLTR] Part of an ATP-driven transport system CT_067/CT_068/CT_069/CT_070 for a metal. Metal-binding component.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The obligate intracellular pathogen Chlamydia (C.) trachomatis is a globally significant cause of sexually transmitted bacterial infections and the leading etiological agent of preventable blindness. The first-row transition metal iron (Fe) plays critical roles in chlamydial cell biology and acquisition of this nutrient is essential for the survival and virulence of the pathogen. Nevertheless, how C. trachomatis acquires Fe from host cells is not well understood, as it lacks genes encoding known siderophore biosynthetic pathways, receptors for host Fe-storage proteins, and the Fe acquisition machinery common to many bacteria. Recent studies have suggested that C. trachomatis directly acquires host Fe via the ATP-binding cassette permease YtgABCD. Here, we characterized YtgA, the periplasmic solute binding protein component of the transport pathway, that has been implicated in scavenging Fe(III) ions. The structure of Fe(III)-bound YtgA was determined at 2.0 A resolution with the bound ion coordinated via a novel geometry (N3O2). This unusual coordination suggested a highly plastic metal-binding site in YtgA capable of interacting with other cations. Biochemical analyses showed that the metal-binding site of YtgA was not restricted to interaction with only Fe(III) ions, but could bind all transition metal ions examined. However, only Mn(II), Fe(II) and Ni(II) ions bound reversibly to YtgA, with Fe being the most abundant cellular transition metal in C. trachomatis Collectively, these findings show that YtgA is the metal-recruiting component of the YtgABCD permease and is most likely involved in acquisition of Fe(II) and Mn(II) from host cells.IMPORTANCE Chlamydia trachomatis is the most common bacterial sexually transmitted infection in developed countries with an estimated global prevalence of 4.2% in the 15 to 49-year age group. Although infection is asymptomatic in more than 80% of infected women, about 10% of cases result in serious disease. Infection by C. trachomatis is dependent on the ability to acquire essential nutrients, such as the transition metal iron, from the host cells. In this study, we show that the iron is the most abundant transition metal in C. trachomatis and report the structural and biochemical properties of the iron-recruiting protein YtgA. Knowledge of the high-resolution structure of YtgA will provide a platform for future structure-based antimicrobial design approaches.

The structure and metal binding properties of Chlamydia trachomatis YtgA.,Luo Z, Neville SL, Campbell R, Morey JR, Menon S, Thomas M, Eijkelkamp BA, Ween MP, Huston WM, Kobe B, McDevitt CA J Bacteriol. 2019 Oct 14. pii: JB.00580-19. doi: 10.1128/JB.00580-19. PMID:31611288<ref>PMID:31611288</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 6nsi" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Chlamydia trachomatis]]
[[Category: Large Structures]]
[[Category: Begg SL]]
[[Category: Campbell R]]
[[Category: Kobe B]]
[[Category: Luo Z]]
[[Category: McDevitt CA]]