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Contents |
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* Residue conservation analysis
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Enzyme class:
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E.C.2.3.1.15
- Glycerol-3-phosphate O-acyltransferase.
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Reaction:
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Acyl-CoA + sn-glycerol 3-phosphate = CoA + 1-acyl-sn-glycerol 3-phosphate
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Acyl-CoA
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+
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sn-glycerol 3-phosphate
Bound ligand (Het Group name = )
matches with 60.00% similarity
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=
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CoA
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+
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1-acyl-sn-glycerol 3-phosphate
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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Gene Ontology (GO) functional annotation
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Cellular component
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plastid
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3 terms
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Biological process
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metabolic process
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2 terms
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Biochemical function
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transferase activity
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3 terms
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Acta Crystallogr D Biol Crystallogr
60:13-21
(2004)
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PubMed id:
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Substrate recognition and selectivity of plant glycerol-3-phosphate acyltransferases (GPATs) from Cucurbita moscata and Spinacea oleracea.
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T.Tamada,
M.D.Feese,
S.R.Ferri,
Y.Kato,
R.Yajima,
T.Toguri,
R.Kuroki.
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ABSTRACT
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Stromal glycerol-3-phosphate acyltransferases (GPAT) are responsible for the
selective incorporation of saturated and unsaturated fatty-acyl chains into
chloroplast membranes, which is an important determinant of a plant's ability to
tolerate chilling temperatures. The molecular mechanisms of plant chilling
tolerance were elucidated by creating chimeric GPATs between squash (Cucurbita
moscata, chilling-sensitive) and spinach (Spinacea oleracea, chilling-tolerant)
and the results were interpreted using structural information on squash GPAT
determined by X-ray crystallography at 1.55 A resolution. Enzymatic analysis of
the chimeric GPATs showed that the chimeric GPATs containing the spinach region
from residues 128 to 187 prefer the 18:1 unsaturated fatty acid rather than 16:0
saturated fatty acid. Structure analysis suggests that the size and character of
the cavity that is formed from this region determines the specific recognition
of acyl chains.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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S.Q.Zhu,
H.Zhao,
R.Zhou,
B.H.Ji,
and
X.Y.Dan
(2009).
Substrate Selectivity of Glycerol-3-phosphate Acyl Transferase in Rice.
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J Integr Plant Biol, 51,
1040-1049.
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T.Tamada,
E.Honjo,
Y.Maeda,
T.Okamoto,
M.Ishibashi,
M.Tokunaga,
and
R.Kuroki
(2006).
Homodimeric cross-over structure of the human granulocyte colony-stimulating factor (GCSF) receptor signaling complex.
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Proc Natl Acad Sci U S A, 103,
3135-3140.
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PDB code:
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
code is
shown on the right.
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Links
