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PDBsum entry 1bqa
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Aminotransferase
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PDB id
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1bqa
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Contents |
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* Residue conservation analysis
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Enzyme class:
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E.C.2.6.1.1
- aspartate transaminase.
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Reaction:
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L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate
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L-aspartate
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+
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2-oxoglutarate
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=
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oxaloacetate
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+
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L-glutamate
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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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DOI no:
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Biochemistry
38:905-913
(1999)
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PubMed id:
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Functional and structural analysis of cis-proline mutants of Escherichia coli aspartate aminotransferase.
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L.Birolo,
V.N.Malashkevich,
G.Capitani,
F.De Luca,
A.Moretta,
J.N.Jansonius,
G.Marino.
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ABSTRACT
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To elucidate the role of the two conserved cis-proline residues of aspartate
aminotransferase (AspAT), one double and two single mutants of the enzyme from
Escherichia coli (EcAspAT) were prepared: P138A, P195A and P138A/P195A in which
the two prolines were replaced by alanine. The crystal structures of P195A and
P138A/P195A have been determined at 2.3-2.1 A resolution. The wild-type
geometry, including the cis conformation of the 194-195 peptide bond is retained
upon substitution of proline 195 by alanine, whereas the trans conformation is
adopted at the 137-138 peptide bond. Quite surprisingly, the replacement of each
of the two prolines by alanine does not significantly affect either the activity
or the stability of the protein. All the three mutants follow the same pathway
as the wild type for unfolding equilibrium induced by guanidine hydrochloride
[Herold, M., and Kirschner, K. (1990) Biochemistry 29, 1907-1913]. The kinetics
of renaturation of P195A, where the alanine retains the wild-type cis
conformation, is faster than wild type, whereas renaturation of P138A, which
adopts the trans conformation, is slower. We conclude that cis-prolines seem to
have been retained throughout the evolution of aspartate aminotransferase to
possibly play a subtle role in directing the traffic of intermediates toward the
unique structure of the native state, rather than to respond to the needs for a
specific catalytic or functional role.
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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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D.A.Schultz,
A.M.Friedman,
M.A.White,
and
R.O.Fox
(2005).
The crystal structure of the cis-proline to glycine variant (P114G) of ribonuclease A.
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Protein Sci,
14,
2862-2870.
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PDB code:
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S.Lorenzen,
B.Peters,
A.Goede,
R.Preissner,
and
C.Frömmel
(2005).
Conservation of cis prolyl bonds in proteins during evolution.
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Proteins,
58,
589-595.
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J.A.Osés-Prieto,
M.T.Bengoechea-Alonso,
A.Artigues,
A.Iriarte,
and
M.Martinez-Carrión
(2003).
The nature of the rate-limiting steps in the refolding of the cofactor-dependent protein aspartate aminotransferase.
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J Biol Chem,
278,
49988-49999.
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E.B.Kuettner,
R.Hilgenfeld,
and
M.S.Weiss
(2002).
The active principle of garlic at atomic resolution.
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J Biol Chem,
277,
46402-46407.
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PDB codes:
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L.Birolo,
F.Dal Piaz,
P.Pucci,
and
G.Marino
(2002).
Structural characterization of the M* partly folded intermediate of wild type and P138A aspartate aminotransferase from Escherichia coli.
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J Biol Chem,
277,
17428-17437.
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Y.Xiong,
D.Juminaga,
G.V.Swapna,
W.J.Wedemeyer,
H.A.Scheraga,
and
G.T.Montelione
(2000).
Solution NMR evidence for a cis Tyr-Ala peptide group in the structure of [Pro93Ala] bovine pancreatic ribonuclease A.
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Protein Sci,
9,
421-426.
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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
