This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

2x06

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 07:31, 16 November 2017

SULFOLACTATE DEHYDROGENASE FROM METHANOCALDOCOCCUS JANNASCHII

Structural highlights

2x06 is a 8 chain structure with sequence from Atcc 43067. This structure supersedes the now removed PDB entry 1rfm. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
NonStd Res:
Activity:	D-2-hydroxyacid dehydrogenase (NADP(+)), with EC number 1.1.1.272
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Irimia A, Madern D, Zaccai G, Vellieux FM. Methanoarchaeal sulfolactate dehydrogenase: prototype of a new family of NADH-dependent enzymes. EMBO J. 2004 Mar 24;23(6):1234-44. Epub 2004 Mar 11. PMID:15014443 doi:10.1038/sj.emboj.7600147

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2x06"

@@ Line 1: / Line 1: @@
 ==SULFOLACTATE DEHYDROGENASE FROM METHANOCALDOCOCCUS JANNASCHII==
 <StructureSection load='2x06' size='340' side='right' caption='[[2x06]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <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://oca.weizmann.ac.il/oca-docs/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]</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://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 ==

2x06

From Proteopedia

Revision as of 07:31, 16 November 2017

SULFOLACTATE DEHYDROGENASE FROM METHANOCALDOCOCCUS JANNASCHII

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox