1cqx: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1cqx]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Cupriavidus_necator Cupriavidus necator]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CQX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1CQX FirstGlance]. <br> | <table><tr><td colspan='2'>[[1cqx]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Cupriavidus_necator Cupriavidus necator]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CQX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1CQX FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DGG:1-[GLYCEROLYLPHOSPHONYL]-2-[8-(2-HEXYL-CYCLOPROPYL)-OCTANAL-1-YL]-3-[HEXADECANAL-1-YL]-GLYCEROL'>DGG</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>< | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DGG:1-[GLYCEROLYLPHOSPHONYL]-2-[8-(2-HEXYL-CYCLOPROPYL)-OCTANAL-1-YL]-3-[HEXADECANAL-1-YL]-GLYCEROL'>DGG</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1cqx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cqx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1cqx RCSB], [http://www.ebi.ac.uk/pdbsum/1cqx PDBsum]</span></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=1cqx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cqx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1cqx RCSB], [http://www.ebi.ac.uk/pdbsum/1cqx PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Cupriavidus necator]] | [[Category: Cupriavidus necator]] | ||
[[Category: Cramm, R | [[Category: Cramm, R]] | ||
[[Category: Ermler, U | [[Category: Ermler, U]] | ||
[[Category: Friedrich, B | [[Category: Friedrich, B]] | ||
[[Category: Siddiqui, R A | [[Category: Siddiqui, R A]] | ||
[[Category: Globin fold]] | [[Category: Globin fold]] | ||
[[Category: Helix-flanked five-stranded parallel beta sheet]] | [[Category: Helix-flanked five-stranded parallel beta sheet]] | ||
[[Category: Lipid binding protein]] | [[Category: Lipid binding protein]] | ||
[[Category: Six-stranded antiparallel beta sheet]] | [[Category: Six-stranded antiparallel beta sheet]] | ||
Revision as of 22:38, 22 December 2014
Crystal structure of the flavohemoglobin from Alcaligenes eutrophus at 1.75 A resolutionCrystal structure of the flavohemoglobin from Alcaligenes eutrophus at 1.75 A resolution
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe molecular structure of the flavohemoglobin from Alcaligenes eutrophus has been determined to a resolution of 1.75 A and refined to an R-factor of 19.6%. The protein comprises two fused modules: a heme binding module, which belongs to the globin family, and an FAD binding oxidoreductase module, which adopts a fold like ferredoxin reductase. The most striking deviation of the bacterial globin structure from those of other species is the movement of helix E in a way to provide more space in the vicinity of the distal heme binding site. A comparison with other members of the ferredoxin reductase family shows similar tertiary structures for the individual FAD and NAD binding domains but largely different interdomain orientations. The heme and FAD molecules approach each other to a minimal distance of 6.3 A and adopt an interplanar angle of 80 degrees. The electron transfer from FAD to heme occurs in a predominantly polar environment and may occur directly or be mediated by a water molecule. Crystal structure of the flavohemoglobin from Alcaligenes eutrophus at 1.75 A resolution.,Ermler U, Siddiqui RA, Cramm R, Friedrich B EMBO J. 1995 Dec 15;14(24):6067-77. PMID:8557026[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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