2azl: Difference between revisions

Revision as of 17:32, 21 February 2008

Crystal structure for the mutant F117E of Thermotoga maritima octaprenyl pyrophosphate synthase

OverviewOverview

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.

About this StructureAbout this Structure

2AZL is a Single protein structure of sequence from Thermotoga maritima. Active as Trans-octaprenyltranstransferase, with EC number 2.5.1.11 Full crystallographic information is available from OCA.

ReferenceReference

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

Page seeded by OCA on Thu Feb 21 16:32:38 2008

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OCA

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 ==Overview==
-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.
+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.
 ==About this Structure==
@@ Line 14: / Line 14: @@
 [[Category: Thermotoga maritima]]
 [[Category: Trans-octaprenyltranstransferase]]
-[[Category: Chou, C.C.]]
+[[Category: Chou, C C.]]
-[[Category: Guo, R.T.]]
+[[Category: Guo, R T.]]
-[[Category: Ko, T.P.]]
+[[Category: Ko, T P.]]
-[[Category: Kuo, C.J.]]
+[[Category: Kuo, C J.]]
-[[Category: Liang, P.H.]]
+[[Category: Liang, P H.]]
-[[Category: Sun, H.Y.]]
+[[Category: Sun, H Y.]]
-[[Category: Wang, A.H.]]
+[[Category: Wang, A H.]]
 [[Category: isoprenyl pyrophosphate synthase]]
 [[Category: octaprenyl pyrophosphate synthase]]
@@ Line 27: / Line 27: @@
 [[Category: trans-prenyltransferase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 18:13:13 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:32:38 2008''