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3cky
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3cky]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Eubacterium_barkeri Eubacterium barkeri]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CKY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3CKY FirstGlance]. <br> | <table><tr><td colspan='2'>[[3cky]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Eubacterium_barkeri Eubacterium barkeri]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CKY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3CKY FirstGlance]. <br> | ||
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</td></tr> |
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3cky FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cky OCA], [https://pdbe.org/3cky PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3cky RCSB], [https://www.ebi.ac.uk/pdbsum/3cky PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3cky ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3cky FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cky OCA], [https://pdbe.org/3cky PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3cky RCSB], [https://www.ebi.ac.uk/pdbsum/3cky PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3cky ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [https://www.uniprot.org/uniprot/HMGD_EUBBA HMGD_EUBBA] Catalyzes the conversion of 2-formylglutarate to (S)-2-hydroxymethylglutarate. Has very low activity with (S)-3-hydroxyisobutyrate.<ref>PMID:18680749</ref> | |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</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=3cky ConSurf]. | </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=3cky ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | 2-(Hydroxymethyl)glutarate dehydrogenase, the fourth enzyme of the anaerobic nicotinate fermentation pathway of Eubacterium barkeri, catalyzes the NADH-dependent conversion between (S)-2-formylglutarate and (S)-2-(hydroxymethyl)glutarate. As shown by its 2.3-A crystal structure, this enzyme is a novel member of the beta-hydroxyacid dehydrogenase family and adopts a tetrameric architecture with monomers interacting via their C-terminal catalytic domains. The NAD-binding domains protrude heterogeneously from the central, tetrameric core with domain rotation angles differing up to 12 degrees. Kinetic properties of the enzyme, including NADH inhibition constants, were determined. A strong NADH binding in contrast to weaker NAD(+) binding of the protein was inferred from fluorometrically determined binding constants for the dinucleotide cofactor. The data support either an Iso Ordered Bi Bi mechanism or a more common Ordered Bi Bi mechanism as found in other dehydrogenases. | ||
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| - | Structural and kinetic properties of a beta-hydroxyacid dehydrogenase involved in nicotinate fermentation.,Reitz S, Alhapel A, Essen LO, Pierik AJ J Mol Biol. 2008 Oct 10;382(3):802-11. Epub 2008 Jul 25. PMID:18680749<ref>PMID:18680749</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 3cky" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: 2-hydroxymethylglutarate dehydrogenase]] | ||
[[Category: Eubacterium barkeri]] | [[Category: Eubacterium barkeri]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Alhapel | + | [[Category: Alhapel A]] |
| - | [[Category: Essen | + | [[Category: Essen L-O]] |
| - | [[Category: Pierik | + | [[Category: Pierik AJ]] |
| - | [[Category: Reitz | + | [[Category: Reitz S]] |
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Current revision
Structural and Kinetic Properties of a beta-hydroxyacid dehydrogenase involved in nicotinate fermentation
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