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PDBsum entry 4zwn
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PDB id:
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Hydrolase
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Title:
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Crystal structure of a soluble variant of the monoglyceride lipase from saccharomyces cerevisiae
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Structure:
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Monoglyceride lipase. Chain: a, b, c, d. Fragment: unp residues 2-313. Synonym: mgl,monoacylglycerol hydrolase,mgh,monoacylglycerol lipase, magl,serine hydrolase yju3. Engineered: yes. Mutation: yes
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Source:
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Saccharomyces cerevisiae (strain atcc 204508 / s288c). Baker's yeast. Organism_taxid: 559292. Strain: atcc 204508 / s288c. Gene: yju3, ykl094w, ykl441. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
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Resolution:
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2.49Å
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R-factor:
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0.190
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R-free:
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0.224
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Authors:
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P.Aschauer,S.Rengachari,K.Gruber,M.Oberer
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Key ref:
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P.Aschauer
et al.
(2016).
Crystal structure of the Saccharomyces cerevisiae monoglyceride lipase Yju3p.
Biochim Biophys Acta,
1861,
462-470.
PubMed id:
DOI:
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Date:
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19-May-15
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Release date:
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27-Apr-16
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PROCHECK
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Headers
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References
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P28321
(MGLL_YEAST) -
Monoglyceride lipase from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
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Seq:
Struc:
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313 a.a.
310 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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*
PDB and UniProt seqs differ
at 3 residue positions (black
crosses)
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Enzyme class:
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E.C.3.1.1.23
- acylglycerol lipase.
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Reaction:
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Hydrolyzes glycerol monoesters of long-chain fatty acids.
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DOI no:
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Biochim Biophys Acta
1861:462-470
(2016)
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PubMed id:
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Crystal structure of the Saccharomyces cerevisiae monoglyceride lipase Yju3p.
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P.Aschauer,
S.Rengachari,
J.Lichtenegger,
M.Schittmayer,
K.M.Das,
N.Mayer,
R.Breinbauer,
R.Birner-Gruenberger,
C.C.Gruber,
R.Zimmermann,
K.Gruber,
M.Oberer.
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ABSTRACT
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Monoglyceride lipases (MGLs) are a group of α/β-hydrolases that catalyze the
hydrolysis of monoglycerides (MGs) into free fatty acids and glycerol. This
reaction serves different physiological functions, namely in the last step of
phospholipid and triglyceride degradation, in mammalian endocannabinoid and
arachidonic acid metabolism, and in detoxification processes in microbes.
Previous crystal structures of MGLs from humans and bacteria revealed
conformational plasticity in the cap region of this protein and gave insight
into substrate binding. In this study, we present the structure of a MGL from
Saccharomyces cerevisiae called Yju3p in its free form and in complex with a
covalently bound substrate analog mimicking the tetrahedral intermediate of MG
hydrolysis. These structures reveal a high conservation of the overall shape of
the MGL cap region and also provide evidence for conformational changes in the
cap of Yju3p. The complex structure reveals that, despite the high structural
similarity, Yju3p seems to have an additional opening to the substrate binding
pocket at a different position compared to human and bacterial MGL. Substrate
specificities towards MGs with saturated and unsaturated alkyl chains of
different lengths were tested and revealed highest activity towards MG
containing a C18:1 fatty acid.
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