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PDBsum entry 1rdh
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Hydrolase(endoribonuclease)
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PDB id
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1rdh
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References listed in PDB file
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Key reference
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Title
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Crystallographic analyses of an active HIV-1 ribonuclease h domain show structural features that distinguish it from the inactive form.
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Authors
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D.Chattopadhyay,
B.C.Finzel,
S.H.Munson,
D.B.Evans,
S.K.Sharma,
N.A.Strakalaitus,
D.P.Brunner,
F.M.Eckenrode,
Z.Dauter,
C.Betzel,
H.M.Einspahr.
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Ref.
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Acta Crystallogr D Biol Crystallogr, 1993,
49,
423-427.
[DOI no: ]
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PubMed id
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Abstract
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. An active recombinant preparation of the carboxy-terminal ribonuclease H
(RNase H) domain of HIV-I reverse transcriptase has produced crystals of several
different forms, including a trigonal prism form (P3(1); a = b = 52.03, c =
113.9 A with two molecules per asymmetric unit) and a hexagonal tablet form
(P6(2)22 or P6(4)22; a = b = 93.5, c = 74.1 A with one molecule per asymmetric
unit). The former appears to be isomorphous with crystals of a similar, but
inactive, version of the enzyme that was used for a prior crystal structure
determination [Davies, Hostomska, Hostomsky, Jordan & Matthews (1991).
Science, 252, 88-95]. We have also obtained a structure solution for this
crystal form and have refined it with 2.8 A resolution data (R = 0.216). We
report here details of our crystallization studies and some initial structural
results that verify that the preparation of active HIV-1 RNase H yields a
protein that is not just enzymatically, but also structurally, distinguishable
from the inactive form. Evidence suggests that region 538-542, which may be
involved in the catalytic site and which is disordered in both molecules in the
prior structure determination, is ordered in the crystal structure of the active
enzyme, although the ordering may include more than one conformation for this
loop. It should also be noted that, in the crystal structure of the trigonal
form, RNase H monomers associate to form noncrystallographic twofold-symmetric
dimers by fusing five-stranded mixed beta sheets into a single ten-stranded
dimerwide sheet, an assembly that was not remarked upon by previous
investigators.
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Figure 1.
Fig. 1. Stylized ribbon representations of the two HIV-1 RNase H domains found in the crystallographic asymmetric unit. The two dmains
are related by noncrystallographic twofold axis that is normal to the figure in view (a) and horizontal in the plane of the page in view
(b). The two monomers interact at the outermost strand (~3) of the five-stranded ~ sheet to form a single large sheet that spans both
domains. The position of His539 is indicated.
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The above figure is
reprinted
by permission from the IUCr:
Acta Crystallogr D Biol Crystallogr
(1993,
49,
423-427)
copyright 1993.
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Secondary reference #1
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Title
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Crystal structure of the ribonuclease h domain of HIV-1 reverse transcriptase.
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Authors
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J.F.Davies,
Z.Hostomska,
Z.Hostomsky,
S.R.Jordan,
D.A.Matthews.
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Ref.
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Science, 1991,
252,
88-95.
[DOI no: ]
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PubMed id
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Secondary reference #2
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Title
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A recombinant ribonuclease h domain of HIV-1 reverse transcriptase that is enzymatically active.
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Authors
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D.B.Evans,
K.Brawn,
M.R.Deibel,
W.G.Tarpley,
S.K.Sharma.
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Ref.
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J Biol Chem, 1991,
266,
20583-20585.
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PubMed id
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Headers
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