7ead

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Current revision (13:33, 6 November 2024) (edit) (undo)
 
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<StructureSection load='7ead' size='340' side='right'caption='[[7ead]], [[Resolution|resolution]] 1.74&Aring;' scene=''>
<StructureSection load='7ead' size='340' side='right'caption='[[7ead]], [[Resolution|resolution]] 1.74&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[7ead]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7EAD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7EAD FirstGlance]. <br>
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<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7EAD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7EAD 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]] 1.74&#8491;</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]] 1.74&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEC:HEME+C'>HEC</scene></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEC:HEME+C'>HEC</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=7ead FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ead OCA], [https://pdbe.org/7ead PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ead RCSB], [https://www.ebi.ac.uk/pdbsum/7ead PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ead 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=7ead FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ead OCA], [https://pdbe.org/7ead PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ead RCSB], [https://www.ebi.ac.uk/pdbsum/7ead PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ead ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
 
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[https://www.uniprot.org/uniprot/Q746G4_THET2 Q746G4_THET2]
 
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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Cytochrome c'-beta is a heme protein that belongs to the cytochrome P460 family and consists of homodimeric subunits with a predominantly antiparallel beta-sheet fold. Here, the crystal structure of cytochrome c'-beta from the thermophilic Thermus thermophilus (TTCP-beta) is reported at 1.74 A resolution. TTCP-beta has a typical antiparallel beta-sheet fold similar to that of cytochrome c'-beta from the moderately thermophilic Methylococcus capsulatus (MCCP-beta). The phenylalanine cap structure around the distal side of the heme is also similar in TTCP-beta and MCCP-beta, indicating that both proteins similarly bind nitric oxide and carbon monoxide, as observed spectroscopically. Notably, TTCP-beta exhibits a denaturation temperature of 117 degrees C, which is higher than that of MCCP-beta. Mutational analysis reveals that the increased homodimeric interface area of TTCP-beta contributes to its high thermal stability. Furthermore, 14 proline residues, which are mostly located in the TTCP-beta loop regions, possibly contribute to the rigid loop structure compared with MCCP-beta, which has only six proline residues. These findings, together with those from phylogenetic analysis, suggest that the structures of Thermus cytochromes c'-beta, including TTCP-beta, are optimized for function under the high-temperature conditions in which the source organisms live.
 
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Crystal structure of thermally stable homodimeric cytochrome c'-beta from Thermus thermophilus.,Yoshimi T, Fujii S, Oki H, Igawa T, Adams HR, Ueda K, Kawahara K, Ohkubo T, Hough MA, Sambongi Y Acta Crystallogr F Struct Biol Commun. 2022 Jun 1;78(Pt 6):217-225. doi:, 10.1107/S2053230X22005088. Epub 2022 May 27. PMID:35647678<ref>PMID:35647678</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 7ead" style="background-color:#fffaf0;"></div>
 
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Thermus thermophilus]]
 
[[Category: Adams RH]]
[[Category: Adams RH]]
[[Category: Fujii S]]
[[Category: Fujii S]]

Current revision

Crystal structure of beta-sheet cytochrome c prime from Thermus thermophilus.

PDB ID 7ead

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