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| | ==Crystal structure of methanogen 3-isopropylmalate isomerase small subunit== | | ==Crystal structure of methanogen 3-isopropylmalate isomerase small subunit== |
| - | <StructureSection load='3vba' size='340' side='right' caption='[[3vba]], [[Resolution|resolution]] 2.00Å' scene=''> | + | <StructureSection load='3vba' size='340' side='right'caption='[[3vba]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3vba]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Metja Metja]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VBA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3VBA FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3vba]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Metja Metja]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VBA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VBA FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">leuD, MJ1277 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=243232 METJA])</td></tr> | + | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">leuD, MJ1277 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=243232 METJA])</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=3vba FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vba OCA], [http://pdbe.org/3vba PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3vba RCSB], [http://www.ebi.ac.uk/pdbsum/3vba PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3vba 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=3vba FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vba OCA], [https://pdbe.org/3vba PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vba RCSB], [https://www.ebi.ac.uk/pdbsum/3vba PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vba ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/LEUD_METJA LEUD_METJA]] Enzyme with broad specificity that catalyzes reversible hydroxyacid isomerizations via dehydration/hydration reactions. Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate, a step involved in leucine biosynthesis. Catalyzes the isomerization between 2-methylmalate and 3-methylmalate, via the formation of 2-methylmaleate (citraconate), a step involved in isoleucine biosynthesis. Also displays malease activity, i.e. catalyzes the hydration of maleate to form (R)-malate.<ref>PMID:17449626</ref> | + | [[https://www.uniprot.org/uniprot/LEUD_METJA LEUD_METJA]] Enzyme with broad specificity that catalyzes reversible hydroxyacid isomerizations via dehydration/hydration reactions. Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate, a step involved in leucine biosynthesis. Catalyzes the isomerization between 2-methylmalate and 3-methylmalate, via the formation of 2-methylmaleate (citraconate), a step involved in isoleucine biosynthesis. Also displays malease activity, i.e. catalyzes the hydration of maleate to form (R)-malate.<ref>PMID:17449626</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | + | [[Category: Large Structures]] |
| | [[Category: Metja]] | | [[Category: Metja]] |
| | [[Category: Hwang, K Y]] | | [[Category: Hwang, K Y]] |
| Structural highlights
Function
[LEUD_METJA] Enzyme with broad specificity that catalyzes reversible hydroxyacid isomerizations via dehydration/hydration reactions. Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate, a step involved in leucine biosynthesis. Catalyzes the isomerization between 2-methylmalate and 3-methylmalate, via the formation of 2-methylmaleate (citraconate), a step involved in isoleucine biosynthesis. Also displays malease activity, i.e. catalyzes the hydration of maleate to form (R)-malate.[1]
Publication Abstract from PubMed
3-Isopropylmalate/citramalate (IPM) isomerase catalyzes the second step in the leucine biosynthesis pathway. IPM isomerase from Methanococcus jannaschii is a complex protein consisting of a large (MjLeuC) and a small subunit (MjLeuD). It has broad substrate specificity, unlike other bacterial IPM isomerases. In order to understand the reasons for this broad substrate specificity, we determined the crystal structure of MjLeuD at a resolution of 2.0 A. The asymmetric unit contained 6 molecules of LeuD, including three homodimers. The overall structure had a beta/beta/alpha sandwich-fold consisting of 8 alpha-helices and 7 beta-strands. The C-terminal helix, which is important in homodimer formation, showed conformational differences between two homodimer forms of MjLeuD. In addition, we identified a hydrophobic residue (Val28) near the substrate recognition region that may explain the broad substrate specificity of IPM isomerase. Therefore, we suggest that LeuD proteins can be divided into 2 subfamilies, LeuD subfamilies 1 and 2, which show differences in overall structure and in the substrate recognition region.
Crystal structure of LeuD from Methanococcus jannaschii.,Lee EH, Cho YW, Hwang KY Biochem Biophys Res Commun. 2012 Mar 9;419(2):160-4. Epub 2012 Feb 9. PMID:22326391[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Drevland RM, Waheed A, Graham DE. Enzymology and evolution of the pyruvate pathway to 2-oxobutyrate in Methanocaldococcus jannaschii. J Bacteriol. 2007 Jun;189(12):4391-400. Epub 2007 Apr 20. PMID:17449626 doi:http://dx.doi.org/10.1128/JB.00166-07
- ↑ Lee EH, Cho YW, Hwang KY. Crystal structure of LeuD from Methanococcus jannaschii. Biochem Biophys Res Commun. 2012 Mar 9;419(2):160-4. Epub 2012 Feb 9. PMID:22326391 doi:http://dx.doi.org/10.1016/j.bbrc.2012.01.125
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