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| | ==Periplasmic heme-binding protein RhuT from Roseiflexus sp. RS-1 in two-heme bound form (holo-2)== | | ==Periplasmic heme-binding protein RhuT from Roseiflexus sp. RS-1 in two-heme bound form (holo-2)== |
| - | <StructureSection load='5gj3' size='340' side='right' caption='[[5gj3]], [[Resolution|resolution]] 2.00Å' scene=''> | + | <StructureSection load='5gj3' size='340' side='right'caption='[[5gj3]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5gj3]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Ross1 Ross1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GJ3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5GJ3 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5gj3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Roseiflexus_sp._RS-1 Roseiflexus sp. RS-1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GJ3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5GJ3 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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]] 2Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5giz|5giz]], [[5gj0|5gj0]], [[5gj1|5gj1]], [[5gj2|5gj2]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RoseRS_3565 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=357808 ROSS1])</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=5gj3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gj3 OCA], [https://pdbe.org/5gj3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5gj3 RCSB], [https://www.ebi.ac.uk/pdbsum/5gj3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5gj3 ProSAT]</span></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=5gj3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gj3 OCA], [http://pdbe.org/5gj3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5gj3 RCSB], [http://www.ebi.ac.uk/pdbsum/5gj3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5gj3 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A5UZ69_ROSS1 A5UZ69_ROSS1] |
| | <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: Ross1]] | + | [[Category: Large Structures]] |
| - | [[Category: Nakamura, N]] | + | [[Category: Roseiflexus sp. RS-1]] |
| - | [[Category: Naoe, Y]] | + | [[Category: Nakamura N]] |
| - | [[Category: Rahman, M M]] | + | [[Category: Naoe Y]] |
| - | [[Category: Shiro, Y]] | + | [[Category: Rahman MM]] |
| - | [[Category: Sugimoto, H]] | + | [[Category: Shiro Y]] |
| - | [[Category: Metal transport]]
| + | [[Category: Sugimoto H]] |
| - | [[Category: Transport protein]]
| + | |
| Structural highlights
Function
A5UZ69_ROSS1
Publication Abstract from PubMed
Periplasmic heme-binding proteins (PBPs) in Gram-negative bacteria are components of the heme acquisition system. These proteins shuttle heme across the periplasmic space from outer membrane receptors to ATP-binding cassette (ABC) heme importers located in the inner-membrane. In the present study, we characterized the structures of PBPs found in the pathogen Burkholderia cenocepacia (BhuT) and in the thermophile Roseiflexus sp. RS-1 (RhuT) in the heme-free and heme-bound forms. The conserved motif, in which a well-conserved Tyr interacts with the nearby Arg coordinates on heme iron, was observed in both PBPs. The heme was recognized by its surroundings in a variety of manners including hydrophobic interactions and hydrogen bonds, which was confirmed by isothermal titration calorimetry. Furthermore, this study of 3 forms of BhuT allowed the first structural comparison and showed that the heme-binding cleft of BhuT adopts an "open" state in the heme-free and 2-heme-bound forms, and a "closed" state in the one-heme-bound form with unique conformational changes. Such a conformational change might adjust the interaction of the heme(s) with the residues in PBP and facilitate the transfer of the heme into the translocation channel of the importer.
Structural basis for binding and transfer of heme in bacterial heme-acquisition systems.,Naoe Y, Nakamura N, Rahman MM, Tosha T, Nagatoishi S, Tsumoto K, Shiro Y, Sugimoto H Proteins. 2017 Sep 14. doi: 10.1002/prot.25386. PMID:28913898[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Naoe Y, Nakamura N, Rahman MM, Tosha T, Nagatoishi S, Tsumoto K, Shiro Y, Sugimoto H. Structural basis for binding and transfer of heme in bacterial heme-acquisition systems. Proteins. 2017 Sep 14. doi: 10.1002/prot.25386. PMID:28913898 doi:http://dx.doi.org/10.1002/prot.25386
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