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4ko2
From Proteopedia
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| - | {{STRUCTURE_4ko2| PDB=4ko2 | SCENE= }} | ||
| - | ===Low X-ray dose structure of H2-activated anaerobically purified Dm. baculatum [NiFeSe]-hydrogenase after crystallization under air=== | ||
| - | {{ABSTRACT_PUBMED_23811828}} | ||
| - | == | + | ==Low X-ray dose structure of H2-activated anaerobically purified Dm. baculatum [NiFeSe]-hydrogenase after crystallization under air== |
| - | [[4ko2]] is a 4 chain structure with sequence from [ | + | <StructureSection load='4ko2' size='340' side='right'caption='[[4ko2]], [[Resolution|resolution]] 1.60Å' scene=''> |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4ko2]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Desulfomicrobium_baculatum Desulfomicrobium baculatum] and [https://en.wikipedia.org/wiki/Desulfomicrobium_baculatum_DSM_4028 Desulfomicrobium baculatum DSM 4028]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KO2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4KO2 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]] 1.6Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=FCO:CARBONMONOXIDE-(DICYANO)+IRON'>FCO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=H2S:HYDROSULFURIC+ACID'>H2S</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=SE7:2-AMINO-3-SELENINO-PROPIONIC+ACID'>SE7</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene>, <scene name='pdbligand=UOX:3-(OXIDO-LAMBDA~4~-SELANYL)-L-ALANINE'>UOX</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=4ko2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ko2 OCA], [https://pdbe.org/4ko2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ko2 RCSB], [https://www.ebi.ac.uk/pdbsum/4ko2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ko2 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/PHSS_DESBA PHSS_DESBA] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | This study shows how the NiFeSe site of an anaerobically purified O2-resistant hydrogenase reacts with air to give a seleninate as the first product. Less oxidized states of the active site are readily reduced in the presence of X-rays. Reductive enzyme activation requires an efficient pathway for water escape. | ||
| - | + | Structural foundations for the O2 resistance of Desulfomicrobium baculatum [NiFeSe]-hydrogenase.,Volbeda A, Amara P, Iannello M, De Lacey AL, Cavazza C, Fontecilla-Camps JC Chem Commun (Camb). 2013 Jul 11;49(63):7061-3. doi: 10.1039/c3cc43619e. PMID:23811828<ref>PMID:23811828</ref> | |
| - | <ref | + | |
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 4ko2" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Desulfomicrobium baculatum]] | [[Category: Desulfomicrobium baculatum]] | ||
| - | [[Category: | + | [[Category: Desulfomicrobium baculatum DSM 4028]] |
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Cavazza C]] |
| - | [[Category: | + | [[Category: Fontecilla-Camps JC]] |
| - | + | [[Category: Volbeda A]] | |
| - | [[Category: | + | |
| - | + | ||
Current revision
Low X-ray dose structure of H2-activated anaerobically purified Dm. baculatum [NiFeSe]-hydrogenase after crystallization under air
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