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PDBsum entry 1sud
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Hydrolase(serine proteinase)
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PDB id
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1sud
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* Residue conservation analysis
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Enzyme class:
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E.C.3.4.21.62
- subtilisin.
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Reaction:
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Hydrolysis of proteins with broad specificity for peptide bonds, and a preference for a large uncharged residue in P1. Hydrolyzes peptide amides.
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Proteins
16:205-213
(1993)
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PubMed id:
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Calcium-independent subtilisin by design.
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T.Gallagher,
P.Bryan,
G.L.Gilliland.
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ABSTRACT
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A version of subtilisin BPN' lacking the high affinity calcium site (site A) has
been produced through genetic engineering methods, and its crystal structure
refined at 1.8 A resolution. This protein and the corresponding version
containing the calcium A site are described and compared. The deletion of
residues 75-83 was made in the context of four site-specific replacements
previously shown to stabilize subtilisin. The helix that in wild type is
interrupted by the calcium binding loop, is continuous in the deletion mutant,
with normal geometry. A few residues adjacent to the loop, principally those
that were involved in calcium coordination, are repositioned and/or destabilized
by the deletion. Because refolding is greatly facilitated by the absence of the
Ca-loop, this protein offers a new vehicle for analysis and dissection of the
folding reaction. This is among the largest internal changes to a protein to be
described at atomic resolution.
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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.Kuizon,
K.DiMaiuta,
M.Walus,
E.C.Jenkins,
M.Kuizon,
E.Kida,
A.A.Golabek,
D.O.Espinoza,
R.K.Pullarkat,
and
M.A.Junaid
(2010).
A critical tryptophan and Ca2+ in activation and catalysis of TPPI, the enzyme deficient in classic late-infantile neuronal ceroid lipofuscinosis.
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PLoS One,
5,
e11929.
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C.Ottmann,
R.Rose,
F.Huttenlocher,
A.Cedzich,
P.Hauske,
M.Kaiser,
R.Huber,
and
A.Schaller
(2009).
Structural basis for Ca2+-independence and activation by homodimerization of tomato subtilase 3.
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Proc Natl Acad Sci U S A,
106,
17223-17228.
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PDB codes:
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E.R.Romero-García,
A.Téllez-Valencia,
M.F.Trujillo,
J.G.Sampedro,
H.Nájera,
A.Rojo-Domínguez,
J.García-Soto,
and
M.Pedraza-Reyes
(2009).
Engineering and directed evolution of a Ca2+ binding site A-deficient AprE mutant reveal an essential contribution of the loop Leu75-Leu82 to enzyme activity.
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J Biomed Biotechnol,
2009,
201075.
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O.Almog,
A.González,
N.Godin,
M.de Leeuw,
M.J.Mekel,
D.Klein,
S.Braun,
G.Shoham,
and
R.L.Walter
(2009).
The crystal structures of the psychrophilic subtilisin S41 and the mesophilic subtilisin Sph reveal the same calcium-loaded state.
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Proteins,
74,
489-496.
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PDB codes:
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T.Gallagher,
B.Ruan,
M.London,
M.A.Bryan,
and
P.N.Bryan
(2009).
Structure of a switchable subtilisin complexed with a substrate and with the activator azide.
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Biochemistry,
48,
10389-10394.
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PDB codes:
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S.Tanaka,
K.Saito,
H.Chon,
H.Matsumura,
Y.Koga,
K.Takano,
and
S.Kanaya
(2007).
Crystal structure of unautoprocessed precursor of subtilisin from a hyperthermophilic archaeon: evidence for Ca2+-induced folding.
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J Biol Chem,
282,
8246-8255.
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PDB code:
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M.Pulido,
K.Saito,
S.Tanaka,
Y.Koga,
M.Morikawa,
K.Takano,
and
S.Kanaya
(2006).
Ca2+-dependent maturation of subtilisin from a hyperthermophilic archaeon, Thermococcus kodakaraensis: the propeptide is a potent inhibitor of the mature domain but is not required for its folding.
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Appl Environ Microbiol,
72,
4154-4162.
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S.Tanaka,
K.Saito,
H.Chon,
H.Matsumura,
Y.Koga,
K.Takano,
and
S.Kanaya
(2006).
Crystallization and preliminary X-ray diffraction study of an active-site mutant of pro-Tk-subtilisin from a hyperthermophilic archaeon.
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Acta Crystallogr Sect F Struct Biol Cryst Commun,
62,
902-905.
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N.C.Rockwell,
and
R.S.Fuller
(2002).
Specific modulation of Kex2/furin family proteases by potassium.
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J Biol Chem,
277,
17531-17537.
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O.Almog,
D.T.Gallagher,
J.E.Ladner,
S.Strausberg,
P.Alexander,
P.Bryan,
and
G.L.Gilliland
(2002).
Structural basis of thermostability. Analysis of stabilizing mutations in subtilisin BPN'.
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J Biol Chem,
277,
27553-27558.
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PDB codes:
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P.N.Bryan
(2000).
Protein engineering of subtilisin.
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Biochim Biophys Acta,
1543,
203-222.
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A.Zhou,
S.Martin,
G.Lipkind,
J.LaMendola,
and
D.F.Steiner
(1998).
Regulatory roles of the P domain of the subtilisin-like prohormone convertases.
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J Biol Chem,
273,
11107-11114.
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O.Almog,
T.Gallagher,
M.Tordova,
J.Hoskins,
P.Bryan,
and
G.L.Gilliland
(1998).
Crystal structure of calcium-independent subtilisin BPN' with restored thermal stability folded without the prodomain.
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Proteins,
31,
21-32.
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PDB code:
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R.J.Siezen,
and
J.A.Leunissen
(1997).
Subtilases: the superfamily of subtilisin-like serine proteases.
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Protein Sci,
6,
501-523.
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T.Gallagher,
G.Gilliland,
L.Wang,
and
P.Bryan
(1995).
The prosegment-subtilisin BPN' complex: crystal structure of a specific 'foldase'.
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Structure,
3,
907-914.
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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
codes are
shown on the right.
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Links
