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==HMG-CoA reductase from Methanothermococcus thermolithotrophicus in complex with NADPH at 2.9 A resolution== | |||
<StructureSection load='6hr8' size='340' side='right' caption='[[6hr8]], [[Resolution|resolution]] 2.90Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6hr8]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6HR8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6HR8 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | |||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene></td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Hydroxymethylglutaryl-CoA_reductase_(NADPH) Hydroxymethylglutaryl-CoA reductase (NADPH)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.34 1.1.1.34] </span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6hr8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6hr8 OCA], [http://pdbe.org/6hr8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6hr8 RCSB], [http://www.ebi.ac.uk/pdbsum/6hr8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6hr8 ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
3-hydroxy-3-methylglutaryl-CoA reductase (HMGR) catalyses the last step in mevalonate biosynthesis. HMGR is the target of statin inhibitors that regulate cholesterol concentration in human blood. Here, we report the properties and structures of HMGR from the archaeon Methanothermococcus thermolithotrophicus (mHMGR). The structures of the apoenzyme and the NADPH-complex are highly similar to those of human HMGR. A notable exception is C-terminal helix (Lalpha10-11) that is straight in both mHMGR structures. This helix is kinked and closes the active site in the human enzyme ternary complex, pointing to a substrate-induced structural rearrangement of C-terminal in class-I HMGRs during the catalytic cycle. This article is protected by copyright. All rights reserved. | |||
Crystal structure of archaeal HMG-CoA reductase: insights into structural changes of the C-terminal helix of the class-I enzyme.,Vogeli B, Shima S, Erb T, Wagner T FEBS Lett. 2019 Jan 31. doi: 10.1002/1873-3468.13331. PMID:30702149<ref>PMID:30702149</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6hr8" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Erb, T J]] | |||
[[Category: Shima, S]] | [[Category: Shima, S]] | ||
[[Category: Voegeli, B]] | |||
[[Category: Wagner, T]] | [[Category: Wagner, T]] | ||
[[Category: | [[Category: Cholesterol biosynthesis]] | ||
[[Category: | [[Category: Hmg-coa]] | ||
[[Category: Isoprenoid]] | |||
[[Category: Mevalonate biosynthesis]] | |||
[[Category: Nadph]] | |||
[[Category: Oxidoreductase]] | |||
[[Category: Statin]] | |||
[[Category: Structural rearrangement]] | |||
Revision as of 12:31, 13 February 2019
HMG-CoA reductase from Methanothermococcus thermolithotrophicus in complex with NADPH at 2.9 A resolutionHMG-CoA reductase from Methanothermococcus thermolithotrophicus in complex with NADPH at 2.9 A resolution
Structural highlights
Publication Abstract from PubMed3-hydroxy-3-methylglutaryl-CoA reductase (HMGR) catalyses the last step in mevalonate biosynthesis. HMGR is the target of statin inhibitors that regulate cholesterol concentration in human blood. Here, we report the properties and structures of HMGR from the archaeon Methanothermococcus thermolithotrophicus (mHMGR). The structures of the apoenzyme and the NADPH-complex are highly similar to those of human HMGR. A notable exception is C-terminal helix (Lalpha10-11) that is straight in both mHMGR structures. This helix is kinked and closes the active site in the human enzyme ternary complex, pointing to a substrate-induced structural rearrangement of C-terminal in class-I HMGRs during the catalytic cycle. This article is protected by copyright. All rights reserved. Crystal structure of archaeal HMG-CoA reductase: insights into structural changes of the C-terminal helix of the class-I enzyme.,Vogeli B, Shima S, Erb T, Wagner T FEBS Lett. 2019 Jan 31. doi: 10.1002/1873-3468.13331. PMID:30702149[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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