Journal:Acta Cryst D:S2059798320003101
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| - | <StructureSection load='' size='450' side='right' scene='83/837917/Cv/ | + | <StructureSection load='' size='450' side='right' scene='83/837917/Cv/10' caption=''> |
===The crystal structure of heme ''d<sub>1</sub>'' biosynthesis-associated small c-type cytochrome NirC reveals mixed oligomeric states ''in crystallo''=== | ===The crystal structure of heme ''d<sub>1</sub>'' biosynthesis-associated small c-type cytochrome NirC reveals mixed oligomeric states ''in crystallo''=== | ||
<big>Thomas Klünemann, Steffi Henke and Wulf Blankenfeldt</big> <ref>doi 10.1107/S2059798320003101</ref> | <big>Thomas Klünemann, Steffi Henke and Wulf Blankenfeldt</big> <ref>doi 10.1107/S2059798320003101</ref> | ||
<hr/> | <hr/> | ||
<b>Molecular Tour</b><br> | <b>Molecular Tour</b><br> | ||
| - | NirC is a monoheme c-type cytochrome co-encoded with other proteins involved in nitrite reduction. It possesses the common fold hallmarked of three α-helices that surround a covalently attached heme. Its crystals diffracted anisotropically to a maximum resolution of 2.12 Å (spherical resolution 2.83 Å) and initial phases were obtained by Fe-SAD phasing, revealing the presence of eleven NirC chains in the asymmetric unit. Surprisingly, these protomers arrange into one monomer and two different types of 3D-domain-swapped dimers, one showing pronounced asymmetry. While the simultaneous observation of monomers and dimers probably reflects the interplay between high protein concentration required for crystallization and the structural plasticity of NirC, the identification of conserved structural motifs in the monomer together with a comparison to similar proteins suggest an involvement of NirC in heme ''d<sub>1</sub>'' biosynthesis. | + | NirC is a monoheme c-type cytochrome co-encoded with other proteins involved in nitrite reduction. It possesses the common fold hallmarked of three α-helices that surround a covalently attached heme. Its crystals diffracted anisotropically to a maximum resolution of 2.12 Å (spherical resolution 2.83 Å) and initial phases were obtained by Fe-SAD phasing, revealing the presence of eleven NirC chains in the asymmetric unit (PDB entry [[6tp9]]). Surprisingly, these protomers arrange into one monomer and two different types of 3D-domain-swapped dimers, one showing pronounced asymmetry. While the simultaneous observation of monomers and dimers probably reflects the interplay between high protein concentration required for crystallization and the structural plasticity of NirC, the identification of conserved structural motifs in the monomer together with a comparison to similar proteins suggest an involvement of NirC in heme ''d<sub>1</sub>'' biosynthesis. |
| - | <scene name='83/837917/Cv/ | + | The NirC monomer shown as a cartoon with residues at a maximum distance of 4 Å to the covalently attached heme presented as sticks: |
| + | *<scene name='83/837917/Cv/19'>First view</scene>. | ||
| + | *<scene name='83/837917/Cv/20'>Second view after rotation</scene>. | ||
| + | Colours are based on sequence conservation as defined by Consurf. {{Template:ColorKey_ConSurf_NoYellow_NoGray}} | ||
| + | |||
| + | Depiction of the two different oligomerization states found in the crystal structure of NirC: | ||
| + | *1st oligomerization state <scene name='83/837917/Cv/7'>Far-Dimer</scene>. | ||
| + | *<scene name='83/837917/Cv/8'>Monomer</scene>. | ||
| + | *2nd oligomerization state <scene name='83/837917/Cv/9'>Close-Dimer</scene>. | ||
| + | |||
| + | The residues of the hinge loop: | ||
| + | *<scene name='83/837917/Cv/13'>Far-Dimer</scene>. | ||
| + | *<scene name='83/837917/Cv/15'>Monomer</scene>. | ||
| + | *<scene name='83/837917/Cv/14'>Close-Dimer</scene>. | ||
| + | |||
| + | '''PDB reference:''' c-type cytochrome NirC [[6tp9]] | ||
<b>References</b><br> | <b>References</b><br> | ||
Current revision
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