1v4k: Difference between revisions

New page: left|200px<br /><applet load="1v4k" size="450" color="white" frame="true" align="right" spinBox="true" caption="1v4k, resolution 2.45Å" /> '''Crystal Structure of...
 
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[[Image:1v4k.jpg|left|200px]]<br /><applet load="1v4k" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1v4k.jpg|left|200px]]<br /><applet load="1v4k" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1v4k, resolution 2.45&Aring;" />
caption="1v4k, resolution 2.45&Aring;" />
'''Crystal Structure of Octaprenyl Pyrophosphate Synthase from Hyperthermophilic Thermotoga maritima S77F mutant'''<br />
'''Crystal Structure of Octaprenyl Pyrophosphate Synthase from Hyperthermophilic Thermotoga maritima S77F mutant'''<br />


==Overview==
==Overview==
Octaprenyl pyrophosphate synthase (OPPs) catalyzes consecutive, condensation reactions of farnesyl pyrophosphate (FPP) with isopentenyl, pyrophosphate (IPP) to generate C40 octaprenyl pyrophosphate (OPP), which, constitutes the side chain of bacterial ubiquinone or menaquinone. In this, study, the first structure of long chain C40-OPPs from Thermotoga maritima, has been determined to 2.28-A resolution. OPPs is composed entirely of, alpha-helices joined by connecting loops and is arranged with nine core, helices around a large central cavity. An elongated hydrophobic tunnel, between D and F alpha-helices contains two DDXXD motifs on the top for, substrate binding and is occupied at the bottom with two large residues, Phe-52 and Phe-132. The products of the mutant F132A OPPs are, predominantly C50, longer than the C40 synthesized by the wild-type and, F52A mutant OPPs, suggesting that Phe-132 is the key residue for, determining the product chain length. Ala-76 and Ser-77 located close to, the FPP binding site and Val-73 positioned further down the tunnel were, individually mutated to larger amino acids. A76Y and S77F mainly produce, C20 indicating that the mutated large residues in the vicinity of the FPP, site limit the substrate chain elongation. Ala-76 is the fifth amino acid, upstream from the first DDXXD motif on helix D of OPPs, and its, corresponding amino acid in FPPs is Tyr. In contrast, V73Y mutation led to, additional accumulation of C30 intermediate. The new structure of the, trans-type OPPs, together with the recently determined cis-type UPPs, significantly extends our understanding on the biosynthesis of long chain, polyprenyl molecules.
Octaprenyl pyrophosphate synthase (OPPs) catalyzes consecutive condensation reactions of farnesyl pyrophosphate (FPP) with isopentenyl pyrophosphate (IPP) to generate C40 octaprenyl pyrophosphate (OPP), which constitutes the side chain of bacterial ubiquinone or menaquinone. In this study, the first structure of long chain C40-OPPs from Thermotoga maritima has been determined to 2.28-A resolution. OPPs is composed entirely of alpha-helices joined by connecting loops and is arranged with nine core helices around a large central cavity. An elongated hydrophobic tunnel between D and F alpha-helices contains two DDXXD motifs on the top for substrate binding and is occupied at the bottom with two large residues Phe-52 and Phe-132. The products of the mutant F132A OPPs are predominantly C50, longer than the C40 synthesized by the wild-type and F52A mutant OPPs, suggesting that Phe-132 is the key residue for determining the product chain length. Ala-76 and Ser-77 located close to the FPP binding site and Val-73 positioned further down the tunnel were individually mutated to larger amino acids. A76Y and S77F mainly produce C20 indicating that the mutated large residues in the vicinity of the FPP site limit the substrate chain elongation. Ala-76 is the fifth amino acid upstream from the first DDXXD motif on helix D of OPPs, and its corresponding amino acid in FPPs is Tyr. In contrast, V73Y mutation led to additional accumulation of C30 intermediate. The new structure of the trans-type OPPs, together with the recently determined cis-type UPPs, significantly extends our understanding on the biosynthesis of long chain polyprenyl molecules.


==About this Structure==
==About this Structure==
1V4K is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Trans-octaprenyltranstransferase Trans-octaprenyltranstransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.11 2.5.1.11] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1V4K OCA].  
1V4K is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Trans-octaprenyltranstransferase Trans-octaprenyltranstransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.11 2.5.1.11] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V4K OCA].  


==Reference==
==Reference==
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[[Category: Thermotoga maritima]]
[[Category: Thermotoga maritima]]
[[Category: Trans-octaprenyltranstransferase]]
[[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: Shr, H.L.]]
[[Category: Shr, H L.]]
[[Category: Wang, A.H.J.]]
[[Category: Wang, A H.J.]]
[[Category: SO4]]
[[Category: SO4]]
[[Category: thermophilic]]
[[Category: thermophilic]]
[[Category: trans-type prenyltransferase]]
[[Category: trans-type prenyltransferase]]


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