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3vba
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 3vba is ON HOLD Authors: Hwang, K.Y., Lee, E.H. Description: Crystal structure of methanogen 3-isopropylmalate isomerase small subunit) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of methanogen 3-isopropylmalate isomerase small subunit== | |
| + | <StructureSection load='3vba' size='340' side='right'caption='[[3vba]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3vba]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii_DSM_2661 Methanocaldococcus jannaschii DSM 2661]. 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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</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> | ||
| + | == Function == | ||
| + | [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> | ||
| - | + | ==See Also== | |
| - | + | *[[Isopropylmalate isomerase|Isopropylmalate isomerase]] | |
| - | + | == References == | |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Methanocaldococcus jannaschii DSM 2661]] | ||
| + | [[Category: Hwang KY]] | ||
| + | [[Category: Lee EH]] | ||
Current revision
Crystal structure of methanogen 3-isopropylmalate isomerase small subunit
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