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| | ==Recombinant wild type Nitrosomonas europaea cytochrome c552== | | ==Recombinant wild type Nitrosomonas europaea cytochrome c552== |
| - | <StructureSection load='4jcg' size='340' side='right' caption='[[4jcg]], [[Resolution|resolution]] 1.63Å' scene=''> | + | <StructureSection load='4jcg' size='340' side='right'caption='[[4jcg]], [[Resolution|resolution]] 1.63Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4jcg]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Nitrosomonas_europaea_atcc_19718 Nitrosomonas europaea atcc 19718]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JCG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4JCG FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4jcg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Nitrosomonas_europaea_ATCC_19718 Nitrosomonas europaea ATCC 19718]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JCG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4JCG FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEC:HEME+C'>HEC</scene></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]] 1.63Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cyt, cyt_c552, NE0102 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=228410 Nitrosomonas europaea ATCC 19718])</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4jcg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jcg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4jcg RCSB], [http://www.ebi.ac.uk/pdbsum/4jcg PDBsum]</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=4jcg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jcg OCA], [https://pdbe.org/4jcg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4jcg RCSB], [https://www.ebi.ac.uk/pdbsum/4jcg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4jcg ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/CY552_NITEU CY552_NITEU] Monoheme c-type cytochrome. Probable electron donor to membrane cytochrome oxidase and to periplasmic nitrite reductase. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | </div> | | </div> |
| | + | <div class="pdbe-citations 4jcg" style="background-color:#fffaf0;"></div> |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Nitrosomonas europaea atcc 19718]] | + | [[Category: Large Structures]] |
| - | [[Category: Bren, K L]] | + | [[Category: Nitrosomonas europaea ATCC 19718]] |
| - | [[Category: Can, M]] | + | [[Category: Bren KL]] |
| - | [[Category: Krucinska, J]] | + | [[Category: Can M]] |
| - | [[Category: Wedekind, J E]] | + | [[Category: Krucinska J]] |
| - | [[Category: Cytc domain]]
| + | [[Category: Wedekind JE]] |
| - | [[Category: Electron transport]]
| + | |
| - | [[Category: Heme]]
| + | |
| Structural highlights
Function
CY552_NITEU Monoheme c-type cytochrome. Probable electron donor to membrane cytochrome oxidase and to periplasmic nitrite reductase.
Publication Abstract from PubMed
Nitrosomonas europaea cytochrome c-552 (Ne c-552) variants with the same His/Met axial ligand set but with different EPR spectra have been characterized structurally, to aid understanding of how molecular structure determines heme electronic structure. Visible light absorption, Raman, and resonance Raman spectroscopy of the protein crystals was performed along with structure determination. The structures solved are those of Ne c-552, which displays a "HALS" (or highly anisotropic low-spin) EPR spectrum, and of the deletion mutant Ne N64Delta, which has a rhombic EPR spectrum. Two X-ray crystal structures of wild-type Ne c-552 are reported; one is of the protein isolated from N. europaea cells (Ne c-552n, 2.35 A resolution), and the other is of recombinant protein expressed in Escherichia coli (Ne c-552r, 1.63 A resolution). Ne N64Delta crystallized in two different space groups, and two structures are reported [monoclinic (2.1 A resolution) and hexagonal (2.3 A resolution)]. Comparison of the structures of the wild-type and mutant proteins reveals that heme ruffling is increased in the mutant; increased ruffling is predicted to yield a more rhombic EPR spectrum. The 2.35 A Ne c-552n structure shows 18 molecules in the asymmetric unit; analysis of the structure is consistent with population of more than one axial Met configuration, as seen previously by NMR. Finally, the mutation was shown to yield a more hydrophobic heme pocket and to expel water molecules from near the axial Met. These structures reveal that heme pocket residue 64 plays multiple roles in regulating the axial ligand orientation and the interaction of water with the heme. These results support the hypothesis that more ruffled hemes lead to more rhombic EPR signals in cytochromes c with His/Met axial ligation.
Structural Characterization of Nitrosomonas europaea Cytochrome c-552 Variants with Marked Differences in Electronic Structure.,Can M, Krucinska J, Zoppellaro G, Andersen NH, Wedekind JE, Hersleth HP, Andersson KK, Bren KL Chembiochem. 2013 Jul 31. doi: 10.1002/cbic.201300118. PMID:23908017[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Can M, Krucinska J, Zoppellaro G, Andersen NH, Wedekind JE, Hersleth HP, Andersson KK, Bren KL. Structural Characterization of Nitrosomonas europaea Cytochrome c-552 Variants with Marked Differences in Electronic Structure. Chembiochem. 2013 Jul 31. doi: 10.1002/cbic.201300118. PMID:23908017 doi:10.1002/cbic.201300118
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