4itu | pdb_00004itu

Crystal structure of S-2-HYDROXYPROPYL COENZYME M DEHYDROGENASE (S-HPCDH) bound to S-HPC AND NADH

spinqualitylabelsall models 4itu, resolution 1.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4itu is a 4 chain structure with sequence from Xanthobacter autotrophicus Py2. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.6Å Ligands: 1HS, NAI Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function HCDS3_XANP2 Involved in aliphatic epoxide carboxylation (PubMed:20302306). Catalyzes the reversible oxidation of (2S)-2-hydroxypropyl-coenzyme M (S-HPC) to 2-oxopropyl-coenzyme M (2-KPC) (PubMed:20302306). The enzyme is highly specific for the S enantiomers (PubMed:20302306). In vitro can also use the aliphatic ketone 2-butanone and the aliphatic alcohol 2-propanol, and shows an inherent stereoselectivity for 2-butanone reduction (PubMed:20302306). Publication Abstract from PubMed (R)- and (S)-hydroxypropyl-coenzyme M dehydrogenases (R- and S-HPCDH) are stereospecific enzymes that are central to the metabolism of propylene and epoxide in Xanthobacter autotrophicus. The bacterium produces R- and S-HPCDH simultaneously to facilitate transformation of R- and S-enantiomers of epoxypropane to a common achiral product 2-ketopropyl-CoM (2-KPC). Both R- and S-HPCDH are highly specific for their respective substrates as each enzyme displays less than 0.5% activity with the opposite substrate isomer. In order to elucidate the structural basis for stereospecificity displayed by R- and S-HPCDH we have determined substrate bound crystal structures of S-HPCDH to 1.6A resolution. Comparisons to the previously reported product-bound structure of R-HPCDH reveal that although the placement of catalytic residues within the active site of each enzyme is nearly identical, structural differences in the surrounding area provide each enzyme with a distinct substrate binding pocket. These structures demonstrate how chiral discrimination by R- and S-HPCDH results from alternative binding of the distal end of substrates within each substrate binding pocket. Crystal structures of S-HPCDH reveal determinants of stereospecificity for R- and S-hydroxypropyl-coenzyme M dehydrogenases.,Bakelar JW, Sliwa DA, Johnson SJ Arch Biochem Biophys. 2013 Mar 6. pii: S0003-9861(13)00068-4. doi:, 10.1016/j.abb.2013.02.017. PMID:23474457 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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