1ogy

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<StructureSection load='1ogy' size='340' side='right'caption='[[1ogy]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
<StructureSection load='1ogy' size='340' side='right'caption='[[1ogy]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1ogy]] is a 16 chain structure with sequence from [https://en.wikipedia.org/wiki/"rhodococcus_capsulatus"_molisch_1907 "rhodococcus capsulatus" molisch 1907]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OGY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OGY FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1ogy]] is a 16 chain structure with sequence from [https://en.wikipedia.org/wiki/Cereibacter_sphaeroides Cereibacter sphaeroides]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OGY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OGY 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>, <scene name='pdbligand=MGD:2-AMINO-5,6-DIMERCAPTO-7-METHYL-3,7,8A,9-TETRAHYDRO-8-OXA-1,3,9,10-TETRAAZA-ANTHRACEN-4-ONE+GUANOSINE+DINUCLEOTIDE'>MGD</scene>, <scene name='pdbligand=MO:MOLYBDENUM+ATOM'>MO</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</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]] 3.2&#8491;</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Nitrate_reductase Nitrate reductase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.7.99.4 1.7.99.4] </span></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>, <scene name='pdbligand=MGD:2-AMINO-5,6-DIMERCAPTO-7-METHYL-3,7,8A,9-TETRAHYDRO-8-OXA-1,3,9,10-TETRAAZA-ANTHRACEN-4-ONE+GUANOSINE+DINUCLEOTIDE'>MGD</scene>, <scene name='pdbligand=MO:MOLYBDENUM+ATOM'>MO</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=1ogy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ogy OCA], [https://pdbe.org/1ogy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ogy RCSB], [https://www.ebi.ac.uk/pdbsum/1ogy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ogy 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=1ogy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ogy OCA], [https://pdbe.org/1ogy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ogy RCSB], [https://www.ebi.ac.uk/pdbsum/1ogy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ogy ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/NAPA_RHOS4 NAPA_RHOS4]] Catalytic subunit of the periplasmic nitrate reductase (NAP). Only expressed at high levels during aerobic growth. NapAB complex receives electrons from the membrane-anchored tetraheme protein NapC, thus allowing electron flow between membrane and periplasm. Essential function for nitrate assimilation and may have a role in anaerobic metabolism. [[https://www.uniprot.org/uniprot/NAPB_RHOSH NAPB_RHOSH]] Electron transfer subunit of the periplasmic nitrate reductase complex NapAB. Receives electrons from the membrane-anchored tetraheme c-type NapC protein and transfers these to NapA subunit, thus allowing electron flow between membrane and periplasm. Essential for periplasmic nitrate reduction with nitrate as the terminal electron acceptor.<ref>PMID:10227138</ref> <ref>PMID:10498715</ref> <ref>PMID:11717511</ref> <ref>PMID:16136296</ref>
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[https://www.uniprot.org/uniprot/NAPA_CERS4 NAPA_CERS4] Catalytic subunit of the periplasmic nitrate reductase complex NapAB. Receives electrons from NapB and catalyzes the reduction of nitrate to nitrite.[HAMAP-Rule:MF_01630]<ref>PMID:14528294</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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<jmolCheckbox>
<jmolCheckbox>
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/og/1ogy_consurf.spt"</scriptWhenChecked>
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/og/1ogy_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
<text>to colour the structure by Evolutionary Conservation</text>
</jmolCheckbox>
</jmolCheckbox>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Rhodococcus capsulatus molisch 1907]]
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[[Category: Cereibacter sphaeroides]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Nitrate reductase]]
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[[Category: Adriano J-M]]
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[[Category: Adriano, J M]]
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[[Category: Alric J]]
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[[Category: Alric, J]]
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[[Category: Arnoux P]]
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[[Category: Arnoux, P]]
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[[Category: Frangioni B]]
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[[Category: Frangioni, B]]
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[[Category: Guigliarelli B]]
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[[Category: Guigliarelli, B]]
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[[Category: Pignol D]]
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[[Category: Pignol, D]]
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[[Category: Sabaty M]]
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[[Category: Sabaty, M]]
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[[Category: Oxidoreductase]]
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Current revision

Crystal structure of the heterodimeric nitrate reductase from Rhodobacter sphaeroides

PDB ID 1ogy

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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