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PDBsum entry 1mpt
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Serine proteinase
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PDB id
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1mpt
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References listed in PDB file
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Key reference
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Title
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Structure of a new alkaline serine protease (m-Protease) from bacillus sp. Ksm-K16.
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Authors
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T.Yamane,
T.Kani,
T.Hatanaka,
A.Suzuki,
T.Ashida,
T.Kobatashi,
S.Ito,
O.Yamashita.
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Ref.
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Acta Crystallogr D Biol Crystallogr, 1995,
51,
199-206.
[DOI no: ]
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PubMed id
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Note In the PDB file this reference is
annotated as "TO BE PUBLISHED".
The citation details given above were identified by an automated
search of PubMed on title and author
names, giving a
percentage match of
95%.
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Abstract
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An alkaline serine protease, M-protease, from Bacillus sp. KSM-K16 has been
crystallized. Two morphologically different crystal forms were obtained. Crystal
data of form 1: space group P2(1)2(1)2(1), a = 47.3, b = 62.5, c = 75.6 A, V =
2.23 x 10(5) A(3), Z = 4 and V(m) = 2.09 A(3) Da(-1). Crystal data of form 2:
space group P2(1)2(1)2(1), a = 75.82 (2), b = 57.79 (2), c = 54.19 (1) A, V =
2.29 (2) x 10(5) A(3), Z = 4 and V(m) = 2.15 A(3) Da(-1). The crystal structure
of M-protease in form 2 has been solved by molecular replacement using the
atomic model of subtilisin Carlsberg (SBC) which is 60% homologous with
M-protease, and refined to the crystallographic R-factor of 0.189 for 7004
reflections with F(o)/sigma(F) > 3 between 7 and 2.4 A resolution. The final
model of M-protease contains 1882 protein atoms, two calcium ions and 44 water
molecules. The three-dimensional structure of M-protease is essentially similar
to other subtilisins of known structure. The 269 C(alpha) positions of
M-protease have an r.m.s. difference of 1.06 A with the corresponding positions
of SBC. The crystal data of form 2 are close to those of SBC, though the
structure determination of form 2 made it clear that it is not isomorphous to
the crystal structure of SBC. The deletions of amino acids occur at the residues
36' and 160'-163' compared with SBC (numerals with primes show the numbering for
SBC). The deletion of the four residues (160'-163') may significantly affect the
lack of isomorphism between M-protease and SBC.
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Figure 2.
Fig. 2. Luzzati plots of R factor
versus
resolution (l/2d). All reflections
in the resolution range 7.0-2.4 A with
Fo
> 3tr(F) are used.
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Figure 10.
Fig. 10.
Stereoviews of the active site in M-protease.
(a) The
2Fo -Fc
electron density contoured at 1.4a level
is superposed. (b) The struc-
ture
in SBC (thin lines) and the
Fo -Fc
electron density contoured at
2o
level are
superposed.
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The above figures are
reprinted
by permission from the IUCr:
Acta Crystallogr D Biol Crystallogr
(1995,
51,
199-206)
copyright 1995.
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