View source for 7zsx


==F32V Cytochrome c prime beta from Methylococcus capsulatus (Bath): CO Complex==
<StructureSection load='7zsx' size='340' side='right'caption='[[7zsx]], [[Resolution|resolution]] 1.77&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7zsx]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Methylococcus_capsulatus_str._Bath Methylococcus capsulatus str. Bath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7ZSX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7ZSX 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]] 1.77&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CMO:CARBON+MONOXIDE'>CMO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=7zsx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7zsx OCA], [https://pdbe.org/7zsx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7zsx RCSB], [https://www.ebi.ac.uk/pdbsum/7zsx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7zsx ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/G1UBD5_METCA G1UBD5_METCA] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The structural basis by which gas-binding heme proteins control their interactions with NO, CO, and O(2) is fundamental to enzymology, biotechnology, and human health. Cytochromes c' (cyts c') are a group of putative NO-binding heme proteins that fall into two families: the well-characterized four alpha helix bundle fold (cyts c'-alpha) and an unrelated family with a large beta-sheet fold (cyts c'-beta) resembling that of cytochromes P460. A recent structure of cyt c'-beta from Methylococcus capsulatus Bath revealed two heme pocket phenylalanine residues (Phe 32 and Phe 61) positioned near the distal gas-binding site. This feature, dubbed the "Phe cap," is highly conserved within the sequences of other cyts c'-beta but is absent in their close homologs, the hydroxylamine-oxidizing cytochromes P460, although some do contain a single Phe residue. Here, we report an integrated structural, spectroscopic, and kinetic characterization of cyt c'-beta from Methylococcus capsulatus Bath complexes with diatomic gases, focusing on the interaction of the Phe cap with NO and CO. Significantly, crystallographic and resonance Raman data show that orientation of the electron-rich aromatic ring face of Phe 32 toward distally bound NO or CO is associated with weakened backbonding and higher off rates. Moreover, we propose that an aromatic quadrupole also contributes to the unusually weak backbonding reported for some heme-based gas sensors, including the mammalian NO sensor, soluble guanylate cyclase. Collectively, this study sheds light on the influence of highly conserved distal Phe residues on heme-gas complexes of cytochrome c'-beta, including the potential for aromatic quadrupoles to modulate NO and CO binding in other heme proteins.

A heme pocket aromatic quadrupole modulates gas binding to cytochrome c'-beta: Implications for NO sensors.,Adams HR, Svistunenko DA, Wilson MT, Fujii S, Strange RW, Hardy ZA, Vazquez PA, Dabritz T, Streblow GJ, Andrew CR, Hough MA J Biol Chem. 2023 Jun;299(6):104742. doi: 10.1016/j.jbc.2023.104742. Epub 2023 , Apr 24. PMID:37100286<ref>PMID:37100286</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7zsx" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Methylococcus capsulatus str. Bath]]
[[Category: Adams HR]]
[[Category: Hough MA]]