1sqc
From Proteopedia
(Difference between revisions)
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<StructureSection load='1sqc' size='340' side='right'caption='[[1sqc]], [[Resolution|resolution]] 2.85Å' scene=''> | <StructureSection load='1sqc' size='340' side='right'caption='[[1sqc]], [[Resolution|resolution]] 2.85Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1sqc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[1sqc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Alicyclobacillus_acidocaldarius Alicyclobacillus acidocaldarius]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SQC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SQC FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LDA:LAURYL+DIMETHYLAMINE-N-OXIDE'>LDA</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.85Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LDA:LAURYL+DIMETHYLAMINE-N-OXIDE'>LDA</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=1sqc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sqc OCA], [https://pdbe.org/1sqc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1sqc RCSB], [https://www.ebi.ac.uk/pdbsum/1sqc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sqc ProSAT]</span></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=1sqc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sqc OCA], [https://pdbe.org/1sqc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1sqc RCSB], [https://www.ebi.ac.uk/pdbsum/1sqc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sqc ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [https://www.uniprot.org/uniprot/SQHC_ALIAD SQHC_ALIAD] Catalyzes the cyclization of squalene into hopene. | |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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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=1sqc ConSurf]. | </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=1sqc ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | The crystal structure of squalene-hopene cyclase from Alicyclobacillus acidocaldarius was determined at 2.9 angstrom resolution. The mechanism and sequence of this cyclase are closely related to those of 2,3-oxidosqualene cyclases that catalyze the cyclization step in cholesterol biosynthesis. The structure reveals a membrane protein with membrane-binding characteristics similar to those of prostaglandin-H2 synthase, the only other reported protein of this type. The active site of the enzyme is located in a large central cavity that is of suitable size to bind squalene in its required conformation and that is lined by aromatic residues. The structure supports a mechanism in which the acid starting the reaction by protonating a carbon-carbon double bond is an aspartate that is coupled to a histidine. Numerous surface alpha helices are connected by characteristic QW-motifs (Q is glutamine and W is tryptophan) that tighten the protein structure, possibly for absorbing the reaction energy without structural damage. | ||
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| - | Structure and function of a squalene cyclase.,Wendt KU, Poralla K, Schulz GE Science. 1997 Sep 19;277(5333):1811-5. PMID:9295270<ref>PMID:9295270</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1sqc" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Squalene-hopene cyclase|Squalene-hopene cyclase]] | *[[Squalene-hopene cyclase|Squalene-hopene cyclase]] | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Alicyclobacillus acidocaldarius]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Schulz | + | [[Category: Schulz GE]] |
| - | [[Category: Wendt | + | [[Category: Wendt KU]] |
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Current revision
SQUALENE-HOPENE-CYCLASE FROM ALICYCLOBACILLUS ACIDOCALDARIUS
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