7kpz: Difference between revisions
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==1.70 A resolution crystal structure of Group A Streptococcus HupZ-V5-His6== | |||
<StructureSection load='7kpz' size='340' side='right'caption='[[7kpz]], [[Resolution|resolution]] 1.70Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7kpz]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_sp. Streptococcus sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7KPZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7KPZ FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.703Å</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=7kpz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7kpz OCA], [https://pdbe.org/7kpz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7kpz RCSB], [https://www.ebi.ac.uk/pdbsum/7kpz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7kpz ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q9A0B9_STRP1 Q9A0B9_STRP1] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
HupZ is an expected heme degrading enzyme in the heme acquisition and utilization pathway in Group A Streptococcus. The isolated HupZ protein containing a C-terminal V5-His6 tag exhibits a weak heme degradation activity. Here, we revisited and characterized the HupZ-V5-His6 protein via biochemical, mutagenesis, protein quaternary structure, UV-vis, EPR, and resonance Raman spectroscopies. The results show that the ferric heme-protein complex did not display an expected ferric EPR signal and that heme binding to HupZ triggered the formation of higher oligomeric states. We found that heme binding to HupZ was an O2-dependent process. The single histidine residue in the HupZ sequence, His111, did not bind to the ferric heme, nor was it involved with the weak heme-degradation activity. Our results do not favor the heme oxygenase assignment because of the slow binding of heme and the newly discovered association of the weak heme degradation activity with the His6-tag. Altogether, the data suggest that the protein binds heme by its His6-tag, resulting in a heme-induced higher-order oligomeric structure and heme stacking. This work emphasizes the importance of considering exogenous tags when interpreting experimental observations during the study of heme utilization proteins. | |||
Heme Binding to HupZ with a C-Terminal Tag from Group A Streptococcus.,Traore ES, Li J, Chiura T, Geng J, Sachla AJ, Yoshimoto F, Eichenbaum Z, Davis I, Mak PJ, Liu A Molecules. 2021 Jan 21;26(3). pii: molecules26030549. doi:, 10.3390/molecules26030549. PMID:33494451<ref>PMID:33494451</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Li | <div class="pdbe-citations 7kpz" style="background-color:#fffaf0;"></div> | ||
[[Category: Liu | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Streptococcus sp]] | |||
[[Category: Li J]] | |||
[[Category: Liu A]] | |||
Latest revision as of 18:29, 18 October 2023
1.70 A resolution crystal structure of Group A Streptococcus HupZ-V5-His61.70 A resolution crystal structure of Group A Streptococcus HupZ-V5-His6
Structural highlights
FunctionPublication Abstract from PubMedHupZ is an expected heme degrading enzyme in the heme acquisition and utilization pathway in Group A Streptococcus. The isolated HupZ protein containing a C-terminal V5-His6 tag exhibits a weak heme degradation activity. Here, we revisited and characterized the HupZ-V5-His6 protein via biochemical, mutagenesis, protein quaternary structure, UV-vis, EPR, and resonance Raman spectroscopies. The results show that the ferric heme-protein complex did not display an expected ferric EPR signal and that heme binding to HupZ triggered the formation of higher oligomeric states. We found that heme binding to HupZ was an O2-dependent process. The single histidine residue in the HupZ sequence, His111, did not bind to the ferric heme, nor was it involved with the weak heme-degradation activity. Our results do not favor the heme oxygenase assignment because of the slow binding of heme and the newly discovered association of the weak heme degradation activity with the His6-tag. Altogether, the data suggest that the protein binds heme by its His6-tag, resulting in a heme-induced higher-order oligomeric structure and heme stacking. This work emphasizes the importance of considering exogenous tags when interpreting experimental observations during the study of heme utilization proteins. Heme Binding to HupZ with a C-Terminal Tag from Group A Streptococcus.,Traore ES, Li J, Chiura T, Geng J, Sachla AJ, Yoshimoto F, Eichenbaum Z, Davis I, Mak PJ, Liu A Molecules. 2021 Jan 21;26(3). pii: molecules26030549. doi:, 10.3390/molecules26030549. PMID:33494451[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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