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| | ==Crystal Structure of the Aldolase-Dehydrogenase Complex from Mycobacterium tuberculosis HRv37== | | ==Crystal Structure of the Aldolase-Dehydrogenase Complex from Mycobacterium tuberculosis HRv37== |
| - | <StructureSection load='4jn6' size='340' side='right' caption='[[4jn6]], [[Resolution|resolution]] 1.93Å' scene=''> | + | <StructureSection load='4jn6' size='340' side='right'caption='[[4jn6]], [[Resolution|resolution]] 1.93Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4jn6]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_tuberculosis"_(zopf_1883)_klein_1884 "bacillus tuberculosis" (zopf 1883) klein 1884]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JN6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4JN6 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4jn6]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JN6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4JN6 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=OXL:OXALATE+ION'>OXL</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=OXL:OXALATE+ION'>OXL</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Rv3534c, MT3638 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 "Bacillus tuberculosis" (Zopf 1883) Klein 1884]), mhpF, Rv3535c, MT3639 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 "Bacillus tuberculosis" (Zopf 1883) Klein 1884])</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=4jn6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jn6 OCA], [https://pdbe.org/4jn6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4jn6 RCSB], [https://www.ebi.ac.uk/pdbsum/4jn6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4jn6 ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/4-hydroxy-2-oxovalerate_aldolase 4-hydroxy-2-oxovalerate aldolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.3.39 4.1.3.39] </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=4jn6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jn6 OCA], [http://pdbe.org/4jn6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4jn6 RCSB], [http://www.ebi.ac.uk/pdbsum/4jn6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4jn6 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/HOA_MYCTU HOA_MYCTU]] Catalyzes the retro-aldol cleavage of 4-hydroxy-2-oxopentanoate to pyruvate and acetaldehyde. Is involved in the meta-cleavage pathway for the degradation of aromatic compounds (By similarity). [[http://www.uniprot.org/uniprot/ACDH_MYCTU ACDH_MYCTU]] Catalyzes the conversion of acetaldehyde to acetyl-CoA, using NAD(+) and coenzyme A. Is the final enzyme in the meta-cleavage pathway for the degradation of aromatic compounds (By similarity). | + | [https://www.uniprot.org/uniprot/HOA_MYCTU HOA_MYCTU] Catalyzes the retro-aldol cleavage of 4-hydroxy-2-oxopentanoate to pyruvate and acetaldehyde. Is involved in the meta-cleavage pathway for the degradation of aromatic compounds (By similarity). |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | ==See Also== | | ==See Also== |
| - | *[[Aldolase|Aldolase]] | + | *[[Aldolase 3D structures|Aldolase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: 4-hydroxy-2-oxovalerate aldolase]] | + | [[Category: Large Structures]] |
| - | [[Category: Carere, J]] | + | [[Category: Mycobacterium tuberculosis]] |
| - | [[Category: Kimber, M S]] | + | [[Category: Carere J]] |
| - | [[Category: McKenna, S E]] | + | [[Category: Kimber MS]] |
| - | [[Category: Seah, S Y.K]] | + | [[Category: McKenna SE]] |
| - | [[Category: Aldolase-dehydrogenase]] | + | [[Category: Seah SYK]] |
| - | [[Category: Lyase-oxidoreductase complex]]
| + | |
| - | [[Category: Rossmann fold]]
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| - | [[Category: Tim barrel]]
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| Structural highlights
Function
HOA_MYCTU Catalyzes the retro-aldol cleavage of 4-hydroxy-2-oxopentanoate to pyruvate and acetaldehyde. Is involved in the meta-cleavage pathway for the degradation of aromatic compounds (By similarity).
Publication Abstract from PubMed
HsaF and HsaG are an aldolase and dehydrogenase from the cholesterol degradation pathway of M. tuberculosis. HsaF could be heterologously expressed and purified as a soluble dimer, but the enzyme was inactive in the absence of HsaG. HsaF catalyzes the aldol cleavage of 4-hydroxy-2-oxoacids to produce pyruvate and an aldehyde. The enzyme requires divalent metals for activity, with a preference for Mn2+. The Km values for 4-hydroxy-2-oxoacids were about 20-fold lower than observed for the aldolase homologue, BphI from the polychlorinated biphenyl degradation pathway. Acetaldehyde and propionaldehyde were channeled directly to the dehydrogenase, HsaG, without export to the bulk solvent where they were transformed to acyl-CoA in an NAD+ and coenzyme A dependent reaction. HsaG is able to utilize aldehydes up to five carbons in length as substrates, with similar catalytic efficiencies. The HsaF-HsaG complex was crystallized and its structure determined to a resolution of 1.93 A. Substitution of Serine 41 in HsaG with isoleucine or aspartate resulted in about 35-fold increase in Km for CoA but only 4-fold increase in Km dephospho-CoA, suggesting that this residue interacts with the 3'-ribose phosphate of CoA. A second protein annotated as a 4-hydroxy-2-oxopentanoic acid aldolase in Mycobacterium tuberculosis (MhpE, Rv3469c) was expressed and purified, but was found to lack aldolase activity. Instead this enzyme was found to possess oxaloacetate decarboxylase activity, consistent with the conservation (with the 4-hydroxy-2-oxoacid aldolases) of residues involved in pyruvate enolate stabilization.
Characterization of an aldolase-dehydrogenase complex from the cholesterol degradation pathway of Mycobacterium tuberculosis.,Carere J, McKenna SE, Kimber MS, Seah SY Biochemistry. 2013 Apr 24. PMID:23614353[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Carere J, McKenna SE, Kimber MS, Seah SY. Characterization of an aldolase-dehydrogenase complex from the cholesterol degradation pathway of Mycobacterium tuberculosis. Biochemistry. 2013 Apr 24. PMID:23614353 doi:http://dx.doi.org/10.1021/bi400351h
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