6e4d: Difference between revisions
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==Atomic structure of Mycobacterium tuberculosis DppA== | |||
<StructureSection load='6e4d' size='340' side='right'caption='[[6e4d]], [[Resolution|resolution]] 1.25Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6e4d]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895] and [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=6E4D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6E4D FirstGlance]. <br> | |||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6e3d|6e3d]]</td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">dppA, ERS007741_01322, ERS023446_02924 ([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='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=6e4d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6e4d OCA], [http://pdbe.org/6e4d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6e4d RCSB], [http://www.ebi.ac.uk/pdbsum/6e4d PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6e4d ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Iron is essential for growth of Mycobacterium tuberculosis (Mtb), but most iron in the human body is stored in heme within hemoglobin. Here, we demonstrate that the substrate-binding protein DppA of the inner membrane Dpp transporter is required for heme and hemoglobin utilization by Mtb. The 1.27 A crystal structure of DppA shows a tetrapeptide bound in the protein core and a large solvent-exposed crevice for heme binding. Mutation of arginine 179 in this cleft eliminates heme binding to DppA and prevents heme utilization by Mtb. The outer membrane proteins PPE36 and PPE62 are also required for heme and hemoglobin utilization, indicating that these pathways converge at the cell surface of Mtb. Albumin, the most abundant blood protein, binds heme specifically and bypasses the requirements for PPE36, PPE62 and Dpp. Thus, our study reveals albumin-dependent and -independent heme uptake pathways, highlighting the importance of iron acquisition from heme for Mtb. | |||
Heme and hemoglobin utilization by Mycobacterium tuberculosis.,Mitra A, Ko YH, Cingolani G, Niederweis M Nat Commun. 2019 Sep 18;10(1):4260. doi: 10.1038/s41467-019-12109-5. PMID:31534126<ref>PMID:31534126</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6e4d" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Bacillus coli migula 1895]] | |||
[[Category: Large Structures]] | |||
[[Category: Cingolani, G]] | [[Category: Cingolani, G]] | ||
[[Category: Ko, Y]] | |||
[[Category: Mitra, A]] | |||
[[Category: Niederweis, M]] | [[Category: Niederweis, M]] | ||
[[Category: | [[Category: Heme-binding]] | ||
[[Category: | [[Category: Metal binding protein]] | ||
[[Category: Periplasmic protein]] | |||
Revision as of 10:47, 6 November 2019
Atomic structure of Mycobacterium tuberculosis DppAAtomic structure of Mycobacterium tuberculosis DppA
Structural highlights
Publication Abstract from PubMedIron is essential for growth of Mycobacterium tuberculosis (Mtb), but most iron in the human body is stored in heme within hemoglobin. Here, we demonstrate that the substrate-binding protein DppA of the inner membrane Dpp transporter is required for heme and hemoglobin utilization by Mtb. The 1.27 A crystal structure of DppA shows a tetrapeptide bound in the protein core and a large solvent-exposed crevice for heme binding. Mutation of arginine 179 in this cleft eliminates heme binding to DppA and prevents heme utilization by Mtb. The outer membrane proteins PPE36 and PPE62 are also required for heme and hemoglobin utilization, indicating that these pathways converge at the cell surface of Mtb. Albumin, the most abundant blood protein, binds heme specifically and bypasses the requirements for PPE36, PPE62 and Dpp. Thus, our study reveals albumin-dependent and -independent heme uptake pathways, highlighting the importance of iron acquisition from heme for Mtb. Heme and hemoglobin utilization by Mycobacterium tuberculosis.,Mitra A, Ko YH, Cingolani G, Niederweis M Nat Commun. 2019 Sep 18;10(1):4260. doi: 10.1038/s41467-019-12109-5. PMID:31534126[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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