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| | <StructureSection load='3qd8' size='340' side='right'caption='[[3qd8]], [[Resolution|resolution]] 3.00Å' scene=''> | | <StructureSection load='3qd8' size='340' side='right'caption='[[3qd8]], [[Resolution|resolution]] 3.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3qd8]] 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=3QD8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QD8 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3qd8]] is a 24 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QD8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QD8 FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">bfrB ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 "Bacillus tuberculosis" (Zopf 1883) Klein 1884])</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3Å</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=3qd8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qd8 OCA], [https://pdbe.org/3qd8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qd8 RCSB], [https://www.ebi.ac.uk/pdbsum/3qd8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qd8 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=3qd8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qd8 OCA], [https://pdbe.org/3qd8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qd8 RCSB], [https://www.ebi.ac.uk/pdbsum/3qd8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qd8 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[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>
| + | [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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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Gupta, R K]] | + | [[Category: Mycobacterium tuberculosis]] |
| - | [[Category: Gupta, V]] | + | [[Category: Gupta RK]] |
| - | [[Category: Khare, G]] | + | [[Category: Gupta V]] |
| - | [[Category: Nangpal, P]] | + | [[Category: Khare G]] |
| - | [[Category: Sauter, N K]] | + | [[Category: Nangpal P]] |
| - | [[Category: Tyagi, A K]] | + | [[Category: Sauter NK]] |
| - | [[Category: Ferritin]]
| + | [[Category: Tyagi AK]] |
| - | [[Category: Iron binding protein]]
| + | |
| - | [[Category: Iron storage]]
| + | |
| - | [[Category: Metal binding protein]]
| + | |
| 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
Ferritins are recognized as key players in the iron storage and detoxification processes. Iron acquisition in the case of pathogenic bacteria has long been established as an important virulence mechanism. Here, we report a 3.0 A crystal structure of a ferritin, annotated as Bacterioferritin B (BfrB), from Mycobacterium tuberculosis (Mtb), the causative agent of tuberculosis that continues to be one of the world's deadliest diseases. Similar to the other members of ferritin family, the Mtb BfrB subunit exhibits the characteristic fold of a four-helical bundle that possesses the ferroxidase catalytic centre. We compare the structure of Mtb BfrB with representatives of the ferritin family belonging to the archaea, eubacteria and eukarya. Unlike most other ferritins, Mtb BfrB has an extended C-terminus. To dissect the role of this extended C-terminus, truncated Mtb BfrB was purified and biochemical studies implicate this region in ferroxidase activity and iron release in addition to providing stability to the protein. Functionally important regions in a protein of known 3D-structure can be determined by estimating the degree of conservation of the amino-acid sites with its close homologues. Based on the comparative studies, we identify the slowly evolving conserved sites as well as the rapidly evolving variable sites and analyze their role in relation to structure and function of Mtb BfrB. Further, electrostatic computations demonstrate that although the electrostatic environment of catalytic residues is preserved within the family, extensive variability is exhibited by residues defining the channels and pores, in all likelihood keeping up with the diverse functions executed by these ferritins in varied environments.
Ferritin Structure from Mycobacterium tuberculosis: Comparative Study with Homologues Identifies Extended C-Terminus Involved in Ferroxidase Activity.,Khare G, Gupta V, Nangpal P, Gupta RK, Sauter NK, Tyagi AK PLoS One. 2011 Apr 8;6(4):e18570. PMID:21494619[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
- ↑ 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
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