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PDBsum entry 3hgp
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* Residue conservation analysis
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Enzyme class:
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E.C.3.4.21.36
- pancreatic elastase.
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Reaction:
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Hydrolysis of proteins, including elastin. Preferential cleavage: Ala-|-Xaa.
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J Am Chem Soc
131:11033-11040
(2009)
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PubMed id:
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Combined high-resolution neutron and X-ray analysis of inhibited elastase confirms the active-site oxyanion hole but rules against a low-barrier hydrogen bond.
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T.Tamada,
T.Kinoshita,
K.Kurihara,
M.Adachi,
T.Ohhara,
K.Imai,
R.Kuroki,
T.Tada.
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ABSTRACT
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To help resolve long-standing questions regarding the catalytic activity of the
serine proteases, the structure of porcine pancreatic elastase has been analyzed
by high-resolution neutron and X-ray crystallography. To mimic the tetrahedral
transition intermediate, a peptidic inhibitor was used. A single large crystal
was used to collect room-temperature neutron data to 1.65 A resolution and X-ray
data to 1.20 A resolution. Another crystal provided a low-temperature X-ray data
set to 0.94 A resolution. The neutron data are to higher resolution than
previously reported for a serine protease and the X-ray data are comparable with
other studies. The neutron and X-ray data show that the hydrogen bond between
His57 and Asp102 (chymotrypsin numbering) is 2.60 A in length and that the
hydrogen-bonding hydrogen is 0.80-0.96 A from the histidine nitrogen. This is
not consistent with a low-barrier hydrogen which is predicted to have the
hydrogen midway between the donor and acceptor atom. The observed interaction
between His57 and Asp102 is essentially a short but conventional hydrogen bond,
sometimes described as a short ionic hydrogen bond. The neutron analysis also
shows that the oxygen of the oxopropyl group of the inhibitor is present as an
oxygen anion rather than a hydroxyl group, supporting the role of the "oxyanion
hole" in stabilizing the tetrahedral intermediate in catalysis.
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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.M.Blum,
S.J.Tomanicek,
H.John,
B.L.Hanson,
H.Rüterjans,
B.P.Schoenborn,
P.Langan,
and
J.C.Chen
(2010).
X-ray structure of perdeuterated diisopropyl fluorophosphatase (DFPase): perdeuteration of proteins for neutron diffraction.
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Acta Crystallogr Sect F Struct Biol Cryst Commun,
66,
379-385.
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PDB code:
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R.Kuroki,
T.Tamada,
K.Kurihara,
T.Ohhara,
and
M.Adachi
(2010).
[Collaborative use of neutron and X-ray for determination of drug target proteins].
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Yakugaku Zasshi,
130,
657-664.
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T.Ono,
Y.Ohara-Nemoto,
Y.Shimoyama,
H.Okawara,
T.Kobayakawa,
T.T.Baba,
S.Kimura,
and
T.K.Nemoto
(2010).
Amino acid residues modulating the activities of staphylococcal glutamyl endopeptidases.
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Biol Chem,
391,
1221-1232.
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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
