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| | ==Mycobacterium tuberculosis ferritin homolog, BfrB== | | ==Mycobacterium tuberculosis ferritin homolog, BfrB== |
| - | <StructureSection load='3uno' size='340' side='right' caption='[[3uno]], [[Resolution|resolution]] 2.50Å' scene=''> | + | <StructureSection load='3uno' size='340' side='right'caption='[[3uno]], [[Resolution|resolution]] 2.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3uno]] is a 24 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_tuberculosis"_(zopf_1883)_klein_1884 "bacillus tuberculosis" (zopf 1883) klein 1884]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UNO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3UNO FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3uno]] is a 24 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_tuberculosis"_(zopf_1883)_klein_1884 "bacillus tuberculosis" (zopf 1883) klein 1884]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UNO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UNO FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3oj5|3oj5]]</td></tr> | + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3oj5|3oj5]]</div></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">bfrB, ftn, MT3949 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 "Bacillus tuberculosis" (Zopf 1883) Klein 1884])</td></tr> | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">bfrB, ftn, MT3949 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 "Bacillus tuberculosis" (Zopf 1883) Klein 1884])</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=3uno FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3uno OCA], [http://pdbe.org/3uno PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3uno RCSB], [http://www.ebi.ac.uk/pdbsum/3uno PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3uno ProSAT]</span></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=3uno FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3uno OCA], [https://pdbe.org/3uno PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3uno RCSB], [https://www.ebi.ac.uk/pdbsum/3uno PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3uno ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/BFRB_MYCTU BFRB_MYCTU]] Iron-storage protein that displays ferroxidase activity, catalyzing the oxidation of Fe(2+) ions into Fe(3+) ions, that can then be deposited as a ferric-oxide mineral core within the central cavity of the protein complex.<ref>PMID:21494619</ref> | + | [[https://www.uniprot.org/uniprot/BFRB_MYCTU BFRB_MYCTU]] Iron-storage protein that displays ferroxidase activity, catalyzing the oxidation of Fe(2+) ions into Fe(3+) ions, that can then be deposited as a ferric-oxide mineral core within the central cavity of the protein complex.<ref>PMID:21494619</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | + | [[Category: Large Structures]] |
| | [[Category: Contreras, H]] | | [[Category: Contreras, H]] |
| | [[Category: Goulding, C W]] | | [[Category: Goulding, C W]] |
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| | [[Category: Iron storage]] | | [[Category: Iron storage]] |
| | [[Category: Oxidoreductase]] | | [[Category: Oxidoreductase]] |
| | + | [[Category: Tbsgc]] |
| Structural highlights
Function
[BFRB_MYCTU] Iron-storage protein that displays ferroxidase activity, catalyzing the oxidation of Fe(2+) ions into Fe(3+) ions, that can then be deposited as a ferric-oxide mineral core within the central cavity of the protein complex.[1]
Publication Abstract from PubMed
Mycobacterium tuberculosis (Mtb) is the causative agent of the deadly disease tuberculosis. Iron acquisition, regulation and storage are critical for the survival of this pathogen within a host. Thus, understanding the mechanisms of iron metabolism in Mtb will shed light on its pathogenic nature, as iron is important for infection. Ferritins are a superfamily of protein nanocages that function in both iron detoxification and storage, and Mtb contains both a predicted ferritin and a bacterioferritin. Here, the cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of the ferritin homolog (Mtb BfrB, Rv3841) is reported. An Mtb BfrB crystal grown at pH 6.5 using the hanging-drop vapor-diffusion technique diffracted to 2.50 A resolution and belonged to space group C2, with unit-cell parameters a=226.2, b=226.8, c=113.7 A, beta=94.7 degrees and with 24 subunits per asymmetric unit. Furthermore, modeling the crystal structure of a homologous ferritin into a low-resolution small-angle X-ray scattering (SAXS) electron-density envelope is consistent with the presence of 24 subunits in the BfrB protein cage quaternary structure.
Crystallization and preliminary X-ray crystallographic analysis of a Mycobacterium tuberculosis ferritin homolog, BfrB.,McMath LM, Habel JE, Sankaran B, Yu M, Hung LW, Goulding CW Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Dec 1;66(Pt 12):1657-61., doi: 10.1107/S1744309110042958. Epub 2010 Nov 26. PMID:21139218[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Khare G, Gupta V, Nangpal P, Gupta RK, Sauter NK, Tyagi AK. Ferritin Structure from Mycobacterium tuberculosis: Comparative Study with Homologues Identifies Extended C-Terminus Involved in Ferroxidase Activity. PLoS One. 2011 Apr 8;6(4):e18570. PMID:21494619 doi:10.1371/journal.pone.0018570
- ↑ McMath LM, Habel JE, Sankaran B, Yu M, Hung LW, Goulding CW. Crystallization and preliminary X-ray crystallographic analysis of a Mycobacterium tuberculosis ferritin homolog, BfrB. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Dec 1;66(Pt 12):1657-61., doi: 10.1107/S1744309110042958. Epub 2010 Nov 26. PMID:21139218 doi:10.1107/S1744309110042958
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