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< | ==GEOMETRY OF TRITERPENE CONVERSION TO PENTACARBOCYCLIC HOPENE== | ||
<StructureSection load='1ump' size='340' side='right'caption='[[1ump]], [[Resolution|resolution]] 2.13Å' scene=''> | |||
You may | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1ump]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Alicyclobacillus_acidocaldarius Alicyclobacillus acidocaldarius]. The December 2007 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Oxidosqualene Cyclase'' by David S. Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2007_12 10.2210/rcsb_pdb/mom_2007_12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UMP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UMP FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.13Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=C8E:(HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE'>C8E</scene>, <scene name='pdbligand=SQA:2-AZASQUALENE'>SQA</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ump FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ump OCA], [https://pdbe.org/1ump PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ump RCSB], [https://www.ebi.ac.uk/pdbsum/1ump PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ump ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/SQHC_ALIAD SQHC_ALIAD] Catalyzes the cyclization of squalene into hopene. | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/um/1ump_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</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=1ump ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The membrane protein squalene-hopene cyclase was cocrystallized with 2-azasqualene and analyzed by X-ray diffraction to 2.13 A resolution. The conformation of this close analog was clearly established, and it agreed with the common textbook presentation. The bound squalene undergoes only small conformational changes during the formation of rings A through D, thus requiring no intermediate. However, ring E formation is hindered by an entropic barrier, which may explain its absence in the steroids. The structure analysis revealed a mobile region between the active center cavity and the membrane, which may melt, opening a passage for squalene and hopene. | |||
Conversion of squalene to the pentacarbocyclic hopene.,Reinert DJ, Balliano G, Schulz GE Chem Biol. 2004 Jan;11(1):121-6. PMID:15113001<ref>PMID:15113001</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1ump" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Squalene-hopene cyclase|Squalene-hopene cyclase]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | |||
== | |||
< | |||
[[Category: Alicyclobacillus acidocaldarius]] | [[Category: Alicyclobacillus acidocaldarius]] | ||
[[Category: Large Structures]] | |||
[[Category: Oxidosqualene Cyclase]] | [[Category: Oxidosqualene Cyclase]] | ||
[[Category: | [[Category: RCSB PDB Molecule of the Month]] | ||
[[Category: Balliano | [[Category: Balliano G]] | ||
[[Category: Reinert | [[Category: Reinert DJ]] | ||
[[Category: Schulz | [[Category: Schulz GE]] | ||
Latest revision as of 15:51, 13 December 2023
GEOMETRY OF TRITERPENE CONVERSION TO PENTACARBOCYCLIC HOPENEGEOMETRY OF TRITERPENE CONVERSION TO PENTACARBOCYCLIC HOPENE
Structural highlights
FunctionSQHC_ALIAD Catalyzes the cyclization of squalene into hopene. 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 PubMedThe membrane protein squalene-hopene cyclase was cocrystallized with 2-azasqualene and analyzed by X-ray diffraction to 2.13 A resolution. The conformation of this close analog was clearly established, and it agreed with the common textbook presentation. The bound squalene undergoes only small conformational changes during the formation of rings A through D, thus requiring no intermediate. However, ring E formation is hindered by an entropic barrier, which may explain its absence in the steroids. The structure analysis revealed a mobile region between the active center cavity and the membrane, which may melt, opening a passage for squalene and hopene. Conversion of squalene to the pentacarbocyclic hopene.,Reinert DJ, Balliano G, Schulz GE Chem Biol. 2004 Jan;11(1):121-6. PMID:15113001[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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