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6vna

From Proteopedia

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Current revision (07:09, 3 April 2024) (edit) (undo)
 
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<StructureSection load='6vna' size='340' side='right'caption='[[6vna]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
<StructureSection load='6vna' size='340' side='right'caption='[[6vna]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6vna]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Pardp Pardp]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6VNA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6VNA FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6vna]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Paracoccus_denitrificans_PD1222 Paracoccus denitrificans PD1222]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6VNA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6VNA FirstGlance]. <br>
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</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Pden_1323, Pden_1574 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=318586 PARDP])</td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</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=6vna FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6vna OCA], [https://pdbe.org/6vna PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6vna RCSB], [https://www.ebi.ac.uk/pdbsum/6vna PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6vna 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=6vna FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6vna OCA], [https://pdbe.org/6vna PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6vna RCSB], [https://www.ebi.ac.uk/pdbsum/6vna PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6vna ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/A1B1N4_PARDP A1B1N4_PARDP]
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Heme oxygenases (HOs) play a critical role in recouping iron from the labile heme pool. The acquisition and liberation of heme iron are especially important for the survival of pathogenic bacteria. All characterized HOs, including those belonging to the HugZ superfamily, preferentially cleave free b-type heme. Another common form of heme found in nature is c-type heme, which is covalently linked to proteinaceous cysteine residues. However, mechanisms for direct iron acquisition from the c-type heme pool are unknown. Here we identify a HugZ homolog from the oligopeptide permease (opp) gene cluster of Paracoccus denitrificans that lacks any observable reactivity with heme b and show that it instead rapidly degrades c-type hemopeptides. This c-type heme oxygenase catalyzes the oxidative cleavage of the model substrate microperoxidase-11 at the beta- and/or delta-meso position(s), yielding the corresponding peptide-linked biliverdin, CO, and free iron. X-ray crystallographic analysis suggests that the switch in substrate specificity from b-to c-type heme involves loss of the N-terminal alpha/beta domain and C-terminal loop containing the coordinating histidine residue characteristic of HugZ homologs, thereby accommodating a larger substrate that provides its own iron ligand. These structural features are also absent in certain heme utilization/storage proteins from human pathogens that exhibit low or no HO activity with free heme. This study thus expands the scope of known iron acquisition strategies to include direct oxidative cleavage of heme-containing proteolytic fragments of c-type cytochromes and helps to explain why certain oligopeptide permeases show specificity for the import of heme in addition to peptides.
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A noncanonical heme oxygenase specific for the degradation of c-type heme.,Li S, Isiorho EA, Owens VL, Donnan PH, Odili CL, Mansoorabadi SO J Biol Chem. 2021 Jan-Jun;296:100666. doi: 10.1016/j.jbc.2021.100666. Epub 2021, Apr 17. PMID:33862082<ref>PMID:33862082</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 6vna" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Pardp]]
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[[Category: Paracoccus denitrificans PD1222]]
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[[Category: Isiorho, E A]]
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[[Category: Isiorho EA]]
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[[Category: Mansoorabadi, S O]]
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[[Category: Mansoorabadi SO]]
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[[Category: Heme]]
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[[Category: Metal binding protein]]
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Current revision

Pden_1323

PDB ID 6vna

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