3vba | pdb_00003vba

Crystal structure of methanogen 3-isopropylmalate isomerase small subunit

spinqualitylabelsall models 3vba, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3vba is a 6 chain structure with sequence from Metja. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Gene: leuD, MJ1277 (METJA) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Isopropylmalate isomerase

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