2x06: Difference between revisions
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<StructureSection load='2x06' size='340' side='right' caption='[[2x06]], [[Resolution|resolution]] 2.50Å' scene=''> | <StructureSection load='2x06' size='340' side='right' caption='[[2x06]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2x06]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1rfm 1rfm]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2X06 OCA]. <br> | <table><tr><td colspan='2'>[[2x06]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1rfm 1rfm]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2X06 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2X06 FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>< | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr> | ||
<tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | ||
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/ | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/(R)-2-hydroxyacid_dehydrogenase (R)-2-hydroxyacid dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.272 1.1.1.272] </span></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=2x06 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2x06 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2x06 RCSB], [http://www.ebi.ac.uk/pdbsum/2x06 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=2x06 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2x06 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2x06 RCSB], [http://www.ebi.ac.uk/pdbsum/2x06 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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Methanoarchaeal sulfolactate dehydrogenase: prototype of a new family of NADH-dependent enzymes.,Irimia A, Madern D, Zaccai G, Vellieux FM EMBO J. 2004 Mar 24;23(6):1234-44. Epub 2004 Mar 11. PMID:15014443<ref>PMID:15014443</ref> | Methanoarchaeal sulfolactate dehydrogenase: prototype of a new family of NADH-dependent enzymes.,Irimia A, Madern D, Zaccai G, Vellieux FM EMBO J. 2004 Mar 24;23(6):1234-44. Epub 2004 Mar 11. PMID:15014443<ref>PMID:15014443</ref> | ||
From | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
== References == | == References == | ||
Revision as of 09:42, 10 October 2014
SULFOLACTATE DEHYDROGENASE FROM METHANOCALDOCOCCUS JANNASCHIISULFOLACTATE DEHYDROGENASE FROM METHANOCALDOCOCCUS JANNASCHII
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 crystal structure of the sulfolactate dehydrogenase from the hyperthermophilic and methanogenic archaeon Methanocaldococcus jannaschii was solved at 2.5 A resolution (PDB id. 1RFM). The asymmetric unit contains a tetramer of tight dimers. This structure, complexed with NADH, does not contain a cofactor-binding domain with 'Rossmann-fold' topology. Instead, the tertiary and quaternary structures indicate a novel fold. The NADH is bound in an extended conformation in each active site, in a manner that explains the pro-S specificity. Cofactor binding involves residues belonging to both subunits within the tight dimers, which are therefore the smallest enzymatically active units. The protein was found to be a homodimer in solution by size-exclusion chromatography, analytical ultracentrifugation and small-angle neutron scattering. Various compounds were tested as putative substrates. The results indicate the existence of a substrate discrimination mechanism, which involves electrostatic interactions. Based on sequence homology and phylogenetic analyses, several other enzymes were classified as belonging to this novel family of homologous (S)-2-hydroxyacid dehydrogenases. Methanoarchaeal sulfolactate dehydrogenase: prototype of a new family of NADH-dependent enzymes.,Irimia A, Madern D, Zaccai G, Vellieux FM EMBO J. 2004 Mar 24;23(6):1234-44. Epub 2004 Mar 11. PMID:15014443[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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