2azk

Crystal structure for the mutant W136E of Sulfolobus solfataricus hexaprenyl pyrophosphate synthase

spinqualitylabelsall models 2azk, resolution 2.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2azk is a 2 chain structure with sequence from Saccharolobus solfataricus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.7Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function HEXPP_SACS2 Catalyzes consecutive E-type condensation of two isopentenyl pyrophosphate (IPP) molecules with an allylic substrate such as geranylgeranyl diphosphate (GGPP), farnesyl diphosphate (FPP) or geranyl diphosphate (GPP) to yield the medium-chain product trans-C30-hexaprenyl pyrophosphate (HexPP). GGPP is the physiological substrate. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Hexaprenyl pyrophosphate synthase (HexPPs) from Sulfolobus solfataricus catalyzes the synthesis of trans-C(30)-hexaprenyl pyrophosphate (HexPP) by reacting two isopentenyl pyrophosphate molecules with one geranylgeranyl pyrophosphate. The crystal structure of the homodimeric C(30)-HexPPs resembles those of other trans-prenyltransferases, including farnesyl pyrophosphate synthase (FPPs) and octaprenyl pyrophosphate synthase (OPPs). In both subunits, 10 core helices are arranged about a central active site cavity. Leu164 in the middle of the cavity controls the product chain length. Two protein conformers are observed in the S. solfataricus HexPPs structure, and the major difference between them occurs in the flexible region of residues 84 to 100. Several helices (alphaI, alphaJ, alphaK, and part of alphaH) and the associated loops have high-temperature factors in one monomer, which may be related to the domain motion that controls the entrance to the active site. Different side chain conformations of Trp136 in two HexPPs subunits result in weaker hydrophobic interactions at the dimer interface, in contrast to the symmetric pi-pi stacking interactions of aromatic side chains found in FPPs and OPPs. Finally, the three-conformer switched model may explain the catalytic process for HexPPs. Homodimeric hexaprenyl pyrophosphate synthase from the thermoacidophilic crenarchaeon Sulfolobus solfataricus displays asymmetric subunit structures.,Sun HY, Ko TP, Kuo CJ, Guo RT, Chou CC, Liang PH, Wang AH J Bacteriol. 2005 Dec;187(23):8137-48. PMID:16291686 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Geranylgeranyl pyrophosphate synthase 3D structures

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