6c75: Difference between revisions
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==Structure of Iron containing alcohol dehydrogenase from Thermococcus thioreducens in a monoclinic crystal form== | |||
<StructureSection load='6c75' size='340' side='right'caption='[[6c75]], [[Resolution|resolution]] 2.40Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6c75]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_baa-394 Atcc baa-394]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6C75 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6C75 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATR:2-MONOPHOSPHOADENOSINE-5-DIPHOSPHATE'>ATR</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene></td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">AMR53_06445, SAMN05216170_0411 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=277988 ATCC BAA-394])</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=6c75 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6c75 OCA], [http://pdbe.org/6c75 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6c75 RCSB], [http://www.ebi.ac.uk/pdbsum/6c75 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6c75 ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
An iron-containing alcohol dehydrogenase (FeADH) from the hyperthermophilic archaeon Thermococcus thioreducens was crystallized in unit cells belonging to space groups P21, P212121 and P43212, and the crystal structures were solved at 2.4, 2.1 and 1.9 A resolution, respectively, by molecular replacement using the FeADH from Thermotoga maritima (Schwarzenbacher et al., 2004) as a model. In the monoclinic and orthorhombic crystals the dehydrogenase (molecular mass 41.5 kDa) existed as a dimer containing a twofold noncrystallographic symmetry axis, which was crystallographic in the tetragonal crystals. In the monoclinic and orthorhombic asymmetric units one molecule contained iron and an NADP molecule, while the other did not. The tetragonal crystals lacked both iron and NADP. The structure is very similar to that of the FeADH from T. maritima (average r.m.s. difference for C(alpha) atoms of 1.8 A for 341 aligned atoms). The iron, which is internally sequestered, is bound entirely by amino acids from one domain: three histidines and one aspartic acid. The coenzyme is in an extended conformation, a feature that is common to the large superfamily of NADH-dependent dehydrogenases that share a classical nucleotide-binding domain. A long broad tunnel passes entirely through the enzyme between the two domains, completely encapsulating the coenzyme. | |||
The structure of an iron-containing alcohol dehydrogenase from a hyperthermophilic archaeon in two chemical states.,Larson SB, Jones JA, McPherson A Acta Crystallogr F Struct Biol Commun. 2019 Apr 1;75(Pt 4):217-226. doi:, 10.1107/S2053230X19001201. Epub 2019 Mar 13. PMID:30950821<ref>PMID:30950821</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6c75" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Alcohol dehydrogenase 3D structures|Alcohol dehydrogenase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Atcc baa-394]] | |||
[[Category: Large Structures]] | |||
[[Category: Larson, S B]] | |||
[[Category: McPherson, A]] | |||
[[Category: Alcohol dehydrogenase]] | |||
[[Category: Iron-containing]] | |||
[[Category: Ogl-20p]] | |||
[[Category: Oxidoreductase]] | |||
Revision as of 09:39, 17 April 2019
Structure of Iron containing alcohol dehydrogenase from Thermococcus thioreducens in a monoclinic crystal formStructure of Iron containing alcohol dehydrogenase from Thermococcus thioreducens in a monoclinic crystal form
Structural highlights
Publication Abstract from PubMedAn iron-containing alcohol dehydrogenase (FeADH) from the hyperthermophilic archaeon Thermococcus thioreducens was crystallized in unit cells belonging to space groups P21, P212121 and P43212, and the crystal structures were solved at 2.4, 2.1 and 1.9 A resolution, respectively, by molecular replacement using the FeADH from Thermotoga maritima (Schwarzenbacher et al., 2004) as a model. In the monoclinic and orthorhombic crystals the dehydrogenase (molecular mass 41.5 kDa) existed as a dimer containing a twofold noncrystallographic symmetry axis, which was crystallographic in the tetragonal crystals. In the monoclinic and orthorhombic asymmetric units one molecule contained iron and an NADP molecule, while the other did not. The tetragonal crystals lacked both iron and NADP. The structure is very similar to that of the FeADH from T. maritima (average r.m.s. difference for C(alpha) atoms of 1.8 A for 341 aligned atoms). The iron, which is internally sequestered, is bound entirely by amino acids from one domain: three histidines and one aspartic acid. The coenzyme is in an extended conformation, a feature that is common to the large superfamily of NADH-dependent dehydrogenases that share a classical nucleotide-binding domain. A long broad tunnel passes entirely through the enzyme between the two domains, completely encapsulating the coenzyme. The structure of an iron-containing alcohol dehydrogenase from a hyperthermophilic archaeon in two chemical states.,Larson SB, Jones JA, McPherson A Acta Crystallogr F Struct Biol Commun. 2019 Apr 1;75(Pt 4):217-226. doi:, 10.1107/S2053230X19001201. Epub 2019 Mar 13. PMID:30950821[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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