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* Residue conservation analysis
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Enzyme class:
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Chains A, B, C, D:
E.C.2.5.1.47
- Cysteine synthase.
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Reaction:
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O3-acetyl-L-serine + H2S = L-cysteine + acetate
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O(3)-acetyl-L-serine
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+
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H(2)S
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=
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L-cysteine
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+
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acetate
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Cofactor:
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Pyridoxal 5'-phosphate
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Pyridoxal 5'-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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Biological process
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metabolic process
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4 terms
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Biochemical function
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catalytic activity
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4 terms
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DOI no:
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Proteins
56:387-391
(2004)
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PubMed id:
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Crystal structure of O-acetylserine sulfhydrylase (TM0665) from Thermotoga maritima at 1.8 A resolution.
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A.Heine,
J.M.Canaves,
F.von Delft,
L.S.Brinen,
X.Dai,
A.M.Deacon,
M.A.Elsliger,
S.Eshaghi,
R.Floyd,
A.Godzik,
C.Grittini,
S.K.Grzechnik,
C.Guda,
L.Jaroszewski,
C.Karlak,
H.E.Klock,
E.Koesema,
J.S.Kovarik,
A.Kreusch,
P.Kuhn,
S.A.Lesley,
D.McMullan,
T.M.McPhillips,
M.A.Miller,
M.D.Miller,
A.Morse,
K.Moy,
J.Ouyang,
R.Page,
A.Robb,
K.Rodrigues,
R.Schwarzenbacher,
T.L.Selby,
G.Spraggon,
R.C.Stevens,
H.van den Bedem,
J.Velasquez,
J.Vincent,
X.Wang,
B.West,
G.Wolf,
K.O.Hodgson,
J.Wooley,
I.A.Wilson.
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ABSTRACT
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Selected figure(s)
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Figure 1.
Figure 1. A: Ribbon diagram of Thermotoga maritima TM0665
O-acetylserine sulfhydrylase color coded from N-terminus (blue)
to C-terminus (red) showing the domain organization and location
of the active site (arrow points towards bound phosphate).
Helices (H1-H15) and  -strands
( 1-
9)
are indicated. The two phosphate molecules bound in the active
site are shown in ball and stick. B: The TM0665 tetramer. C and
D: Schematic representation of the interactions between TM0665
and the phosphate molecules bound to domain A (C) and domain B
(D). Ligand bonds are in purple, protein amino acid bonds are in
orange, and hydrogen-bonds are represented as dashed green lines
with distances in A. Residues implicated in hydrophobic
interactions are represented as barbed circle sections. The
atoms are indicated as follows: carbon (black), nitrogen (blue),
oxygen (red), phosphor (purple), and sulfur (yellow).
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Figure 2.
Figure 2. A: Diagram showing the secondary structure elements
in TM0665 superimposed on its primary sequence. The location of
the -hairpin
formed by -strands
1 and 2 is also depicted. B: Location of the phosphate 1 and
phosphate 2 in the active site of TM0665 O-acetylserine
sulfhydrylase. C: Location of pyridoxal 5  -phosphate
(yellow) and methionine (magenta) in the catalytic site of
O-acetylserine sulfhydrylase from Salmonella typhimurium (PDB:
1d6s).
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The above figures are
reprinted
by permission from John Wiley & Sons, Inc.:
Proteins
(2004,
56,
387-391)
copyright 2004.
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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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M.Goto,
T.Yamauchi,
N.Kamiya,
I.Miyahara,
T.Yoshimura,
H.Mihara,
T.Kurihara,
K.Hirotsu,
and
N.Esaki
(2009).
Crystal structure of a homolog of mammalian serine racemase from Schizosaccharomyces pombe.
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J Biol Chem, 284,
25944-25952.
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PDB codes:
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J.Deville,
J.Rey,
and
M.Chabbert
(2008).
Comprehensive analysis of the helix-X-helix motif in soluble proteins.
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Proteins, 72,
115-135.
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G.Zocher,
U.Wiesand,
and
G.E.Schulz
(2007).
High resolution structure and catalysis of O-acetylserine sulfhydrylase isozyme B from Escherichia coli.
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FEBS J, 274,
5382-5389.
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PDB code:
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S.B.Conners,
E.F.Mongodin,
M.R.Johnson,
C.I.Montero,
K.E.Nelson,
and
R.M.Kelly
(2006).
Microbial biochemistry, physiology, and biotechnology of hyperthermophilic Thermotoga species.
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FEMS Microbiol Rev, 30,
872-905.
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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
codes are
shown on the right.
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Links
