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6kta

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Current revision (10:44, 27 March 2024) (edit) (undo)
 
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<StructureSection load='6kta' size='340' side='right'caption='[[6kta]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
<StructureSection load='6kta' size='340' side='right'caption='[[6kta]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6kta]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6KTA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6KTA FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6kta]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Alkalihalobacillus_halodurans_C-125 Alkalihalobacillus halodurans C-125]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6KTA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6KTA FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
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<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=6kta FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6kta OCA], [http://pdbe.org/6kta PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6kta RCSB], [http://www.ebi.ac.uk/pdbsum/6kta PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6kta ProSAT]</span></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6kta FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6kta OCA], [https://pdbe.org/6kta PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6kta RCSB], [https://www.ebi.ac.uk/pdbsum/6kta PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6kta ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/MNTR_BACHD MNTR_BACHD]] Central regulator of manganese homeostasis.
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[https://www.uniprot.org/uniprot/MNTR_HALH5 MNTR_HALH5] Central regulator of manganese homeostasis.[HAMAP-Rule:MF_00732]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The manganese transport regulator MntR is a metal-ion activated transcriptional repressor of manganese transporter genes to maintain manganese ion homeostasis. MntR, a member of the diphtheria toxin repressor (DtxR) family of metalloregulators, selectively responds to Mn2+ and Cd2+ over Fe2+, Co2+ and Zn2+. The DtxR/MntR family members are well conserved transcriptional repressors that regulate the expression of metal ion uptake genes by sensing the metal ion concentration. MntR functions as a homo-dimer with one metal ion binding site per subunit. Each MntR subunit contains two domains: an N-terminal DNA binding domain, and a C-terminal dimerization domain. However, it lacks the C-terminal SH3-like domain of DtxR/IdeR. The metal ion binding site of MntR is located at the interface of the two domains, whereas the DtxR/IdeR subunit contains two metal ion binding sites, the primary and ancillary sites, separated by 9 A. In this paper, we reported the crystal structures of the apo and Mn2+-bound forms of MntR from Bacillus halodurans, and analyze the structural basis of the metal ion binding site. The crystal structure of the Mn2+-bound form is almost identical to the apo form of MntR. In the Mn2+-bound structure, one subunit contains a binuclear cluster of manganese ions, the A and C sites, but the other subunit forms a mononuclear complex. Structural data about MntR from B. halodurans supports the previous hypothesizes about manganese-specific activation mechanism of MntR homologues.
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Structural analysis of the manganese transport regulator MntR from Bacillus halodurans in apo and manganese bound forms.,Lee MY, Lee DW, Joo HK, Jeong KH, Lee JY PLoS One. 2019 Nov 18;14(11):e0224689. doi: 10.1371/journal.pone.0224689., eCollection 2019. PMID:31738781<ref>PMID:31738781</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 6kta" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Alkalihalobacillus halodurans C-125]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Lee, J Y]]
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[[Category: Lee JY]]
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[[Category: Lee, M Y]]
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[[Category: Lee MY]]
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[[Category: Mntr]]
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[[Category: Transcription]]
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[[Category: Transcription factor]]
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Current revision

Crystal structure of B. halodurans MntR in apo form

PDB ID 6kta

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