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PDBsum entry 1nsf
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Protein transport
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PDB id
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1nsf
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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 the ATP-Dependent oligomerization domain of n-Ethylmaleimide sensitive factor complexed with ATP.
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Authors
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R.C.Yu,
P.I.Hanson,
R.Jahn,
A.T.Brünger.
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Ref.
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Nat Struct Biol, 1998,
5,
803-811.
[DOI no: ]
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PubMed id
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Abstract
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N-ethylmaleimide-sensitive factor (NSF) is a hexameric ATPase which primes
and/or dissociates SNARE complexes involved in intracellular fusion events. Each
NSF protomer contains three domains: an N-terminal domain required for SNARE
binding and two ATPase domains, termed D1 and D2, with D2 being required for
oligomerization. We have determined the 1.9 A crystal structure of the D2 domain
of NSF complexed with ATP using multi-wavelength anomalous dispersion phasing.
D2 consists of a nucleotide binding subdomain with a Rossmann fold and a
C-terminal subdomain, which is structurally unique among nucleotide binding
proteins. There are interactions between the ATP moiety and both the neighboring
D2 protomer and the C-terminal subdomain that may be important for ATP-dependent
oligomerization. Of particular importance are three well-ordered and conserved
lysine residues that form ionic interactions with the beta- and
gamma-phosphates, one of which likely contributes to the low hydrolytic activity
of D2.
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Figure 2.
Figure 2. Magnesium ion, in white, is coordinated by Thr 550,
three water molecules (one of which is coordinated by Asp 603),
and [222]beta - and [223]gamma -phosphate oxygens. Prepared
using gl-render, Bobscript^[224]42, and rendered using
POV-ray^[225]43. a, Stereoview of experimental electron density
map using MAD phases. b, Stereoview of phase-combined 2F[o]-F[c]
*sgr;[A]-weighted electron density maps using MAD and model
phases of the refined model.
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Figure 6.
Figure 6. a,Contact regions between subdomains of a protomer, in
red and orange, and between neighboring protomers, in yellow and
purple. b, The N-terminal and C-terminal subdomains contact
through a hydrophobic patch consisting of Ile 508 and Trp 510
from the former (red), and Ile 670, Leu 682, and Leu 683 from
the latter (orange). c, Between N-terminal subdomains on
neighboring protomers, another hydrophobic contact is formed
between Ile 574, Val 612, and Ile 614 from one protomer (purple)
and the  -
through  -carbons
of Lys 586, Leu 609, Phe 618 and Val 628 from the other (yellow).
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The above figures are
reprinted
by permission from Macmillan Publishers Ltd:
Nat Struct Biol
(1998,
5,
803-811)
copyright 1998.
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Secondary reference #1
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Title
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Domain structure of an n-Ethylmaleimide-Sensitive fusion protein involved in vesicular transport.
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Authors
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M.Tagaya,
D.W.Wilson,
M.Brunner,
N.Arango,
J.E.Rothman.
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Ref.
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J Biol Chem, 1993,
268,
2662-2666.
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PubMed id
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