5esc: Difference between revisions

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Unreleased structure'''
-The entry 5esc is ON HOLD  until Paper Publication
+==Crystal structure of Group A Streptococcus HupZ==
+<StructureSection load='5esc' size='340' side='right'caption='[[5esc]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5esc]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_sp._'group_A' Streptococcus sp. 'group A']. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ESC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ESC 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]] 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=5esc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5esc OCA], [https://pdbe.org/5esc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5esc RCSB], [https://www.ebi.ac.uk/pdbsum/5esc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5esc ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/Q1JHG0_STRPD Q1JHG0_STRPD]
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+In Group A streptococcus (GAS), the metallorepressor MtsR regulates iron homeostasis. Here we describe a new MtsR-repressed gene, which we named hupZ (heme utilization protein). A recombinant HupZ protein was purified bound to heme from Escherichia coli grown in the presence of 5-aminolevulinic acid and iron. HupZ specifically binds heme with stoichiometry of 1:1. The addition of NADPH to heme-bound HupZ (in the presence of cytochrome P450 reductase, NADPH-regeneration system and catalase) triggered progressive decrease of the HupZ Soret band and the appearance of an absorption peak at 660 nm that was resistance to hydrolytic conditions. No spectral changes were observed when ferredoxin and ferredoxin reductase were used as redox partners. Differential spectroscopy with myoglobin or with the ferrous chelator, ferrozine, confirmed that carbon monoxide and free iron are produced during the reaction. ApoHupZ was crystallized as a homodimer with a split beta-barrel conformation in each monomer comprising six beta strands and three alpha helices. This structure resembles the split beta-barrel domain shared by the members of a recently described family of heme degrading enzymes. However, HupZ is smaller and lacks key residues found in the proteins of the latter group. Phylogenetic analysis places HupZ on a clade separated from those for previously described heme oxygenases. In summary, we have identified a new GAS enzyme-containing split beta-barrel and capable of heme biotransformation in vitro; to the best of our knowledge, this is the first enzyme among Streptococcus species with such activity.
-Authors: Agniswamy, J., Weber, I.T.
+In vitro heme biotransformation by the HupZ enzyme from Group A streptococcus.,Sachla AJ, Ouattara M, Romero E, Agniswamy J, Weber IT, Gadda G, Eichenbaum Z Biometals. 2016 May 6. PMID:27154580<ref>PMID:27154580</ref>
-Description: Crystal structure of Group A Streptococcus HupZ
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Weber, I.T]]
+<div class="pdbe-citations 5esc" style="background-color:#fffaf0;"></div>
-[[Category: Agniswamy, J]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Streptococcus sp. 'group A']]
+[[Category: Agniswamy J]]
+[[Category: Weber IT]]