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| | <StructureSection load='4kia' size='340' side='right'caption='[[4kia]], [[Resolution|resolution]] 1.75Å' scene=''> | | <StructureSection load='4kia' size='340' side='right'caption='[[4kia]], [[Resolution|resolution]] 1.75Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4kia]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Lismo Lismo]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KIA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4KIA FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4kia]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Listeria_monocytogenes_EGD-e Listeria monocytogenes EGD-e]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KIA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4KIA FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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]] 1.75Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">lmo2213 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=169963 LISMO])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=4kia FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kia OCA], [http://pdbe.org/4kia PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4kia RCSB], [http://www.ebi.ac.uk/pdbsum/4kia PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4kia 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=4kia FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kia OCA], [https://pdbe.org/4kia PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4kia RCSB], [https://www.ebi.ac.uk/pdbsum/4kia PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4kia ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/HMO_LISMO HMO_LISMO] Catalyzes the degradation of heme to biliverdin in the presence of a suitable electron donor such as ascorbate, with the subsequent release of iron. Hardly any CO is released by the heme degradation reaction. Binds heme (PubMed:24598731). Allows bacterial pathogens to use the host heme as an iron source. Release of iron from heme may play a crucial role in the pathogenicity of L.monocytogenes (Probable).<ref>PMID:24598731</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: Lismo]] | + | [[Category: Listeria monocytogenes EGD-e]] |
| - | [[Category: Duong, T]] | + | [[Category: Duong T]] |
| - | [[Category: Kim, K K]] | + | [[Category: Kim KK]] |
| - | [[Category: Kim, T]] | + | [[Category: Kim T]] |
| - | [[Category: Ferredoxin fold]]
| + | |
| - | [[Category: Heme binding]]
| + | |
| - | [[Category: Heme-degrading enzyme]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| Structural highlights
Function
HMO_LISMO Catalyzes the degradation of heme to biliverdin in the presence of a suitable electron donor such as ascorbate, with the subsequent release of iron. Hardly any CO is released by the heme degradation reaction. Binds heme (PubMed:24598731). Allows bacterial pathogens to use the host heme as an iron source. Release of iron from heme may play a crucial role in the pathogenicity of L.monocytogenes (Probable).[1]
Publication Abstract from PubMed
Bacterial pathogens have evolved diverse types of efficient machinery to acquire haem, the most abundant source of iron in the human body, and degrade it for the utilization of iron. Gram-positive bacteria commonly encode IsdG-family proteins as haem-degrading monooxygenases. Listeria monocytogenes is predicted to possess an IsdG-type protein (Lmo2213), but the residues involved in haem monooxygenase activity are not well conserved and there is an extra N-terminal domain in Lmo2213. Therefore, its function and mechanism of action cannot be predicted. In this study, the crystal structure of Lmo2213 was determined at 1.75 A resolution and its haem-binding and haem-degradation activities were confirmed. Structure-based mutational and functional assays of this protein, designated as an Isd-type L. monocytogenes haem-degrading enzyme (Isd-LmHde), identified that Glu71, Tyr87 and Trp129 play important roles in haem degradation and that the N-terminal domain is also critical for its haem-degrading activity. The haem-degradation product of Isd-LmHde is verified to be biliverdin, which is also known to be the degradation product of other bacterial haem oxygenases. This study, the first structural and functional report of the haem-degradation system in L. monocytogenes, sheds light on the concealed haem-utilization system in this life-threatening human pathogen.
Structural and functional characterization of an Isd-type haem-degradation enzyme from Listeria monocytogenes.,Duong T, Park K, Kim T, Kang SW, Hahn MJ, Hwang HY, Jang I, Oh HB, Kim KK Acta Crystallogr D Biol Crystallogr. 2014 Mar;70(Pt 3):615-26. doi:, 10.1107/S1399004713030794. Epub 2014 Feb 15. PMID:24598731[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Duong T, Park K, Kim T, Kang SW, Hahn MJ, Hwang HY, Jang I, Oh HB, Kim KK. Structural and functional characterization of an Isd-type haem-degradation enzyme from Listeria monocytogenes. Acta Crystallogr D Biol Crystallogr. 2014 Mar;70(Pt 3):615-26. doi:, 10.1107/S1399004713030794. Epub 2014 Feb 15. PMID:24598731 doi:http://dx.doi.org/10.1107/S1399004713030794
- ↑ Duong T, Park K, Kim T, Kang SW, Hahn MJ, Hwang HY, Jang I, Oh HB, Kim KK. Structural and functional characterization of an Isd-type haem-degradation enzyme from Listeria monocytogenes. Acta Crystallogr D Biol Crystallogr. 2014 Mar;70(Pt 3):615-26. doi:, 10.1107/S1399004713030794. Epub 2014 Feb 15. PMID:24598731 doi:http://dx.doi.org/10.1107/S1399004713030794
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