2azl

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(New page: 200px<br /><applet load="2azl" size="350" color="white" frame="true" align="right" spinBox="true" caption="2azl, resolution 2.80&Aring;" /> '''Crystal structure fo...)
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[[Image:2azl.gif|left|200px]]<br /><applet load="2azl" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="2azl, resolution 2.80&Aring;" />
 
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'''Crystal structure for the mutant F117E of Thermotoga maritima octaprenyl pyrophosphate synthase'''<br />
 
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==Overview==
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==Crystal structure for the mutant F117E of Thermotoga maritima octaprenyl pyrophosphate synthase==
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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.
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<StructureSection load='2azl' size='340' side='right'caption='[[2azl]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2azl]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AZL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2AZL FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2azl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2azl OCA], [https://pdbe.org/2azl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2azl RCSB], [https://www.ebi.ac.uk/pdbsum/2azl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2azl ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q9X1M1_THEMA Q9X1M1_THEMA]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/az/2azl_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2azl ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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==About this Structure==
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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<ref>PMID:16291686</ref>
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2AZL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. 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=2AZL OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16291686 16291686]
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</div>
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[[Category: Single protein]]
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<div class="pdbe-citations 2azl" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Thermotoga maritima]]
[[Category: Thermotoga maritima]]
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[[Category: Trans-octaprenyltranstransferase]]
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[[Category: Chou CC]]
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[[Category: Chou, C.C.]]
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[[Category: Guo RT]]
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[[Category: Guo, R.T.]]
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[[Category: Ko TP]]
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[[Category: Ko, T.P.]]
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[[Category: Kuo CJ]]
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[[Category: Kuo, C.J.]]
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[[Category: Liang PH]]
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[[Category: Liang, P.H.]]
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[[Category: Sun HY]]
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[[Category: Sun, H.Y.]]
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[[Category: Wang AH]]
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[[Category: Wang, A.H.]]
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[[Category: isoprenyl pyrophosphate synthase]]
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[[Category: octaprenyl pyrophosphate synthase]]
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[[Category: octaprenyl-diphosphate synthase]]
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[[Category: opps]]
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[[Category: trans-prenyltransferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 18:13:13 2008''
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Current revision

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

PDB ID 2azl

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