3u99

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<StructureSection load='3u99' size='340' side='right'caption='[[3u99]], [[Resolution|resolution]] 1.15&Aring;' scene=''>
<StructureSection load='3u99' size='340' side='right'caption='[[3u99]], [[Resolution|resolution]] 1.15&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3u99]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Sheb5 Sheb5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3U99 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3U99 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3u99]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Shewanella_baltica_OS155 Shewanella baltica OS155]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3U99 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3U99 FirstGlance]. <br>
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</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>
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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]] 1.146&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2fw5|2fw5]], [[2fwt|2fwt]], [[2czs|2czs]], [[1jni|1jni]]</div></td></tr>
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<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>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Sbal_0241 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=325240 SHEB5])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3u99 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u99 OCA], [https://pdbe.org/3u99 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3u99 RCSB], [https://www.ebi.ac.uk/pdbsum/3u99 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3u99 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=3u99 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u99 OCA], [https://pdbe.org/3u99 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3u99 RCSB], [https://www.ebi.ac.uk/pdbsum/3u99 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3u99 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/A3CZ62_SHEB5 A3CZ62_SHEB5]
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Multiheme cytochromes c (cyts c) are c-type cyts characterized by non-standard structural and spectroscopic properties. The relative disposition of the heme cofactors in the core of these proteins is conserved and they can be classified from their geometry in two main groups. In one group the porphyrin planes are arranged in a perpendicular fashion, while in the other they are parallel. Orientation of the heme groups is a key factor that regulates the intramolecular electron transfer pathway. A 16.5 kDa diheme cyt c, isolated from the bacterium Shewanella baltica OS155 (Sb-DHC), was cloned and expressed in E. coli and its structure was investigated by X-ray crystallography. Using high-resolution data (1.14 A) collected at ELETTRA (Trieste), the crystal structure, with an orthorhombic cell (a = 40.81, b = 42.97, c = 82.07 A), was solved using the homologous diheme from Rhodobacter sphaeroides (Rs-DHC) as the initial model. The electron density map of the refined structure (Rfact of 13.8% and Rfree of 15.4%) shows a two domain structure connected by a central unstructured region (N72-G87). The Sb-DHC, like its homologue (Rs-DHC), folds into a new cyt c class: the N-terminal globular domain, with its three alpha-helices, belongs to class I of c-type cyts, while the C-terminal domain includes a rare pi-helix. The metal centre of the c-type heme groups is axially coordinated by two His residues and it is covalently bound to the protein through two Cys bonds.
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High-resolution crystal structure of the recombinant diheme cytochrome c from Shewanella baltica (OS155).,De March M, Di Rocco G, Hickey N, Geremia S J Biomol Struct Dyn. 2014 Feb 21. PMID:24559494<ref>PMID:24559494</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 3u99" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[Cytochrome C 3D structures|Cytochrome C 3D structures]]
*[[Cytochrome C 3D structures|Cytochrome C 3D structures]]
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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: Sheb5]]
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[[Category: Shewanella baltica OS155]]
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[[Category: Geremia, S]]
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[[Category: De March M]]
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[[Category: March, M De]]
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[[Category: Di Rocco G]]
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[[Category: Rocco, G Di]]
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[[Category: Geremia S]]
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[[Category: Bacterium shewanella baltica os155]]
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[[Category: Cytochrome c fold]]
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[[Category: Diheme protein]]
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[[Category: Electron transfer protein]]
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[[Category: Electron transport]]
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Revision as of 13:51, 14 March 2024

The experimental X-ray structure of the new diheme cytochrome type c from Shewanella baltica OS155 sb-DHC

PDB ID 3u99

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