9fxc: Difference between revisions

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'''Unreleased structure'''


The entry 9fxc is ON HOLD  until Paper Publication
==Cryo-EM structure of IrtAB in inward-facing state in nanodisc==
 
<StructureSection load='9fxc' size='340' side='right'caption='[[9fxc]], [[Resolution|resolution]] 3.60&Aring;' scene=''>
Authors:  
== Structural highlights ==
 
<table><tr><td colspan='2'>[[9fxc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycolicibacterium_thermoresistibile_ATCC_19527 Mycolicibacterium thermoresistibile ATCC 19527]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9FXC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9FXC FirstGlance]. <br>
Description:  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.6&#8491;</td></tr>
[[Category: Unreleased Structures]]
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AGS:PHOSPHOTHIOPHOSPHORIC+ACID-ADENYLATE+ESTER'>AGS</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=9fxc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9fxc OCA], [https://pdbe.org/9fxc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9fxc RCSB], [https://www.ebi.ac.uk/pdbsum/9fxc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9fxc ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/IRTA_MYCT3 IRTA_MYCT3] Part of the ABC transporter complex IrtAB involved in the import of iron-bound mycobactin (Fe-MBT) and carboxymycobactin (Fe-cMBT) (PubMed:32296173). Has a preference for Fe-MBT over Fe-cMBT (PubMed:32296173). Mycobactins are then reduced by the siderophore interaction domain to facilitate iron release in the bacterial cell (PubMed:32296173). Transmembrane domains (TMD) form a pore in the membrane and the ATP-binding domain (NBD) is responsible for energy generation (PubMed:32296173).<ref>PMID:32296173</ref>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mycolicibacterium thermoresistibile ATCC 19527]]
[[Category: Gonda I]]
[[Category: Seeger MA]]
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