2x06
From Proteopedia
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- | [[Image:2x06.png|left|200px]] | ||
- | < | + | ==SULFOLACTATE DEHYDROGENASE FROM METHANOCALDOCOCCUS JANNASCHII== |
- | + | <StructureSection load='2x06' size='340' side='right'caption='[[2x06]], [[Resolution|resolution]] 2.50Å' scene=''> | |
- | You may | + | == Structural highlights == |
- | + | <table><tr><td colspan='2'>[[2x06]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43067 Atcc 43067]. 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://proteopedia.org/fgij/fg.htm?mol=2X06 FirstGlance]. <br> | |
- | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</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 id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/D-2-hydroxyacid_dehydrogenase_(NADP(+)) D-2-hydroxyacid dehydrogenase (NADP(+))], 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 id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2x06 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2x06 OCA], [http://pdbe.org/2x06 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2x06 RCSB], [http://www.ebi.ac.uk/pdbsum/2x06 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2x06 ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [[http://www.uniprot.org/uniprot/COMC_METJA COMC_METJA]] Catalyzes the reduction of sulfopyruvate to (R)-sulfolactate much more efficiently than the reverse reaction. Also catalyzes the reduction of oxaloacetate, alpha-ketoglutarate, and to a much lower extent, KHTCA, but not pyruvate. Involved in the biosynthesis of both coenzyme M (with (R)-sulfolactate) and methanopterin (with alpha-ketoglutarate). | ||
+ | == Evolutionary Conservation == | ||
+ | [[Image:Consurf_key_small.gif|200px|right]] | ||
+ | Check<jmol> | ||
+ | <jmolCheckbox> | ||
+ | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/x0/2x06_consurf.spt"</scriptWhenChecked> | ||
+ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
+ | <text>to colour the structure by Evolutionary Conservation</text> | ||
+ | </jmolCheckbox> | ||
+ | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2x06 ConSurf]. | ||
+ | <div style="clear:both"></div> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | The 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<ref>PMID:15014443</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
- | + | <div class="pdbe-citations 2x06" style="background-color:#fffaf0;"></div> | |
- | + | == References == | |
- | + | <references/> | |
- | + | __TOC__ | |
- | + | </StructureSection> | |
- | + | [[Category: Atcc 43067]] | |
- | + | [[Category: Large Structures]] | |
- | + | [[Category: Irimia, A]] | |
- | + | [[Category: Madern, D]] | |
- | < | + | [[Category: Vellieux, F M.D]] |
- | [[Category: | + | [[Category: Zaccai, G]] |
- | [[Category: Irimia, A | + | |
- | [[Category: Madern, D | + | |
- | [[Category: Vellieux, F M.D | + | |
- | [[Category: Zaccai, G | + | |
[[Category: Coenzyme m]] | [[Category: Coenzyme m]] | ||
[[Category: Coenzyme m biosynthesis]] | [[Category: Coenzyme m biosynthesis]] |
Current revision
SULFOLACTATE DEHYDROGENASE FROM METHANOCALDOCOCCUS JANNASCHII
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